Crystals of the tyrosine kinase domain of non-insulin receptor tyrosine kinases

ABSTRACT

Crystals of the tyrosine kinase domain of cytoplasmic tyrosine kinases and receptor tyrosine kinases that undergo ligand-mediated receptor dimerization are provided. In particular, crystals of a mutant of the tyrosine kinase domain of fibroblast growth factor receptor 1 (FLGK), alone and in complex with a non-hydrolyzable adenosine triphosphate analogue, are provided. Also provided are the high resolution three dimensional structures of crystalline FLGK, both alone and in co-complex with the adenosine triphosphate analogue, as determined by X-ray diffraction.

1. INTRODUCTION

[0001] The present invention concerns crystalline forms of polypeptides corresponding to the catalytic domain of receptor tyrosine kinases of the non-insulin receptor type. Such tyrosine kinases include receptors of a class that are not covalently cross-linked but are understood to undergo ligand-induced dimerization (such as the FGF-receptor), as well as cytoplasmic tyrosine kinases. The invention also concerns methods for obtaining such crystals and to the high-resolution X-ray diffraction structures and atomic structure coordinates obtained therefrom. The crystals of the invention, and the atomic structure coordinates obtained therefrom, are useful for solving the crystal and solution structures of the tyrosine kinase domains and for identifying compounds that bind to domains of receptor and non-receptor tyrosine kinases.

2. BACKGROUND OF THE INVENTION

[0002] Growth factors play important roles in the control of cell growth, differentiation, metabolism and oncogenesis. The signals generated by a growth factor are transduced across the cellular membrane by transmembrane receptors specific for the growth factor. The diverse biological effects of growth factors are mediated by a large family of cell surface transmembrane receptors with intrinsic protein tyrosine kinase (PTK) activity. The extracellular portion of receptor PTKs contain the binding site for its particular growth factor/ligand, whereas the tyrosine kinase activity resides in the cytoplasmic portion. Binding of a growth factor to the extracellular domain of this receptor results in autophosphorylation of specific tyrosine residues in the cytoplasmic domain. These phosphotyrosines either stimulate PTK activity or serve as binding sites for downstream signalling proteins containing Src-homology 2 (SH2) or phosphotyrosine binding (PTB) domains.

[0003] Eighteen classes or subfamilies of human receptor PTKs have been identified to date, including the insulin receptor (IR), EGF-receptor, PDGF receptor and FGF-receptor. Ligand-induced dimerization of receptors such as the EGF, PDGF and FGF receptors is thought to be essential for activation. Growth factors, such as PDGF are dimeric molecules which, by themselves, are able to induce PDGF-receptor dimerization. However, FGFs are monomeric and are unable, by themselves, to induce receptor dimerization. Dimerization of FGF receptors is thought to be mediated by FGF in concert with heparin sulfate proteoglycans (soluble or cell surface bound).

[0004] In contrast to the EGF, PDGF and FGF receptors, which are monomeric and dimerize upon ligand binding, the insulin receptor exists as a “dimer.” In fact, the insulin receptor is a disulphide-linked α₂β₂ heterotetramer. Binding of insulin to the extracellular α-chains is thought to cause a change within the quaternary structure of the receptor that results in autophosphorylation of specific tyrosines in the cytoplasmic portion of the β chains.

[0005] In an effort to elucidate the mechanisms underlying kinase activation, the crystal structure of such proteins is often sought to be determined. The crystal structures of several protein serine/threonine kinases have been reported: cyclic-AMP-dependent protein kinase (CAPK; Knighton et al., 1994); cyclin-dependent kinase 2 (CDK2; DeBondt et al., 1993); mitogen-activated protein kinase (MAPK; Zhang et al., 1994); and twitchin kinase (Hu et al., 1994). However, the crystalline structure of only one receptor tyrosine kinase has been determined—the unphosphorylated apo form of the tyrosine kinase domain of the insulin receptor (Hubbard et al., 1994).

[0006] Despite these reports, the ability to obtain crystalline forms of the tyrosine kinase domains of non-insulin receptor tyrosine kinases; i.e., cytoplasmic tyrosine kinases and/or receptor tyrosine kinases that undergo ligand-mediated dimerization, has not been realized. A particularly illuminating example is the EGF receptor; to the Applicant's knowledge, researchers armed with the knowledge of how to obtain crystals of the tyrosine kinase domains of both the insulin receptor and serine/threonine kinases have attempted to obtain crystals of the tyrosine kinase domain of EGF receptor without success.

3. SUMMARY OF THE INVENTION

[0007] The invention relates to crystalline forms of polypeptides corresponding to the catalytic domains of receptor tyrosine kinases of the non-insulin receptor type. Such tyrosine kinases include receptors that are not covalently cross-linked, but are believed to undergo ligand-induced dimerization, as well as cytoplasmic tyrosine kinases. The polypeptides of the invention include, but are not limited to, crystallized polypeptides corresponding to the native or mutated catalytic domain of tyrosine kinases (i.e., the non-insulin receptor-type described above), derivative crystals (ie., heavy atom derivatives), and co-crystals of the native or mutated catalytic domain in association with one or more compounds, including but not limited to cofactors, substrates, substrate analogs, inhibitors, allosteric effectors, etc., and preferably compounds that bind the catalytic site.

[0008] Preferably, the crystalline catalytic domains of the invention are of sufficient quality to provide for a determination of the three-dimensional X-ray diffraction structure of the crystalline polypeptide to a resolution of about 1.5 Å to about 2.5 Å.

[0009] The invention is based, in part, on the Applicants' discovery and elucidation of the sequence requirements for the successful crystallization of polypeptides corresponding to catalytic domains of receptor tyrosine kinases that are not covalently cross-linked and are believed to undergo ligand-induced dimerization—a goal which heretofore remained elusive. In this regard, the. Applicants have determined that at least about 20 amino acid residues (+/−5 amino acid residues) upstream of the first glycine in the conserved glycine-rich region of the catalytic domain, and at least about 17 amino acid residues (+/−5 amino acid residues) downstream of the conserved arginine located at the C-terminal boundary of the catalytic domain are required to engineer a polypeptide suitable for crystallization.

[0010] In those cases where the resulting polypeptide contains cysteine residues that interfere with crystallization, such cysteine residues can be substituted with an appropriate amino acid that does not readily form covalent bonds with other amino acid residues under crystallization conditions, e.g., such substitutions include, but are not limited to Ala, Ser, or Gly. Any cysteines located in a non-helical or non-β-strand segment based on secondary structural assignments are candidates for replacement. Cysteines located in domains corresponding to the glycine-rich loop, the kinase insert, the juxtamembrane region or the activation loop are prime candidates for replacement. However, substitutions of cysteine residues that are conserved among the kinases should be avoided (e.g., substitutions of the highly conserved cysteine residues located at the C-terminus, positions 725 and 736 in FIG. 6A, should be avoided).

[0011] The invention is demonstrated by way of example, for the fibroblast growth factor (FGF) receptor-1 (FGF-R1). The examples demonstrate that the crystal structure of the tyrosine kinase domain of the FGF-1 has-been determined to 2.0 Å resolution; the crystal structure of the FGF-R1 catalytic domainin complex with an ATP analog is described to 2.3 Åresolution.

[0012] The crystalline catalytic domains are useful for elucidating the mechanism by which the receptor tyrosine kinases are activated by ligand-induced dimerization, and for the identification of compounds that bind to the catalytic domain.

3.1 Definitions

[0013] As used herein, the following terms shall have the following meanings:

[0014] “Native Tyrosine Kinase Domain or Native Catalytic Domain:” As used herein, “native tyrosine kinase domain” or “native catalytic domain” refers to that portion or domain of a naturally occurring cytoplasmic tyrosine kinase or non-insulin receptor tyrosine kinase which possesses protein. tyrosine kinase (“PTK”) activity as described in Mohammadi et al., 1991 and 1996.

[0015] “Human FLGK:” As used herein, “human FLGK” refers to the tyrosine kinase domain of human fibroblast growth factor receptor 1 (“FGFR1”) having the amino acid sequence of SEQ ID. NO:1. Generally, human FLGK comprises-a 310 amino acid residue fragment (residues 456 to 765) of human FGFR1.

[0016] “FLGK:” As used herein, “FLGK” refers to a mutant of human FLGK which is characterized by the amino acid sequence of SEQ ID NO:2. As compared to human FLGK, FLGK contains the following amino acid substitutions: Cys-488→Ala, Cys-584→Ser, Leu→457→Val, and has an additional five amino acid residues at the N-terminus (Ser-Ala-Ala-Gly-Thr).

[0017] “Mutant:” As used herein, “mutant” refers to a polypeptide which is obtained by replacing at least one amino acid residue in a native tyrosine kinase domain with a different amino acid residue and/or by adding and/or deleting amino acid residues within the native polypeptide or at the N- and/or C-terminus of a polypeptide corresponding to a native tyrosine kinase domain and which has substantially the same three-dimensional structure as the native tyrosine kinase domain from which it is derived. By having substantially the same three-dimensional structure is meant having a set of atomic structure coordinates that have a root mean square deviation (r.m.s.d.) of less than or equal to about 2 Å when superimposed with the atomic structure coordinates of the native tyrosine kinase domain from which the mutant is derived when at least about 50% to 100% of the Cα atoms of the native tyrosine kinase are included in the superposition.

[0018] A mutant may have, but need not have, PTK activity.

[0019] “Crystal:” As used herein, “crystal” refers to a polypeptide in crystalline form. The term “crystal” includes native crystals, derivative crystals and co-crystals, as described herein.

[0020] “Native Crystal:” As used herein, “native crystal” refers to a crystal wherein the polypeptide is substantially pure.

[0021] “Derivative Crystal:” As used herein, “derivative crystal” refers to a crystal wherein the polypeptide is in covalent association with one or more heavy-metal atoms.

[0022] “Co-Crystal:” As used herein, “co-crystal” refers to a crystal wherein the polypeptide is in association with one or more compounds. Such compounds include, by way of example and not limitation, cofactors, substrates, substrate analogues, inhibitors, allosteric effectors, etc. Preferred compounds include AMP-PCP and AMP-PNP.

[0023] “Co-Complex:” As used herein, “co-complex” refers to a polypeptide in association with one or more compounds as enumerated above.

[0024] “Association:” As used herein, “association” refers to a condition of proximity between a chemical entity or compound, or portions or fragments thereof, and tyrosine kinase domain protein, or portions or fragments thereof. The association may be non-covalent, i.e., where the juxtaposition is energetically favored by, e.g., hydrogen-bonding, van der Waals, electrostatic or hydrophobic interactions, or it may be covalent.

[0025] “Active Site:” As used herein, “active site” refers to that site in tyrosine kinase domains where substrate peptide binding, ATP binding and cleavage occur. For human FLGK and FLGK, the active site comprises the catalytic loop, the activation loop and the nucleotide binding loop and is characterized by at least amino acid residues Lys-514, Glu-531, Asp-623, Asn-628, the glycine-rich loop (amino acid residues 485-490), Asp-641 and Arg-627 (FIG. 3).

[0026] “Catalytic Loop:” As used herein, “catalytic loop” refers to a loop in tyrosine kinase domains between αE and β7 containing conserved amino acid residues that are believed to be important in the phosphotransfer reaction or enzymatic process. For human FLGK and FLGK the catalytic loop contains aspartic acid residue Asp-623, which acts as a catalytic base, and is characterized by at least amino acid residues 621 to 628 (FIG. 3).

[0027] “Activation Loop:” As used herein, “activation loop” refers to a loop in tyrosine kinase domains between ⊖8 and αEF that is believed to act as a regulatory loop. For human FLGK and FLGK, the activation loop contains two autophosphorylation sites and is characterized by at least amino acid residues 640 to 663 (FIG. 3).

[0028] “Nucleotide Binding Loon or Glycine-Rich Loon:” As used herein, “nucleotide-binding loop” or “glycine-rich loop” refers to a loop in tyrosine kinase domains between β1 and β2 which contains the protein kinase-conserved glycine-rich GXGXXG consensus sequence (where X is any amino acid). For human FLGK and FLGK the nucleotide binding loop is characterized by at least amino acid residues 485 to 490 (FIG. 3).

[0029] “Autophosphorylation Site:” As used herein, “autophosphorylation site” refers to those tyrosine residues in tyrosine kinase domains that are phosphorylated by a tyrosine kinase domain. Human FLGK and FLGK have six (6) autophosphorylation sites: two in the activation loop (Tyr-653 and Tyr-654), one in the juxtamembrane region (Tyr-463), two in the kinase insert (Tyr-583 and Tyr-585) and one in the C-terminal lobe (Tyr-730) (Mohammadi et al., 1996).

[0030] “Juktamembrane Recion:” As used herein, “juxtamembrane region” refers to that portion of receptor tyrosine kinases located between the transmembrane helix and the tyrosine kinase domain. For human FGFR1 the juxtamembrane region is characterized by at least amino acid residues 398 to 470 (FIG. 6).

[0031] “Kinase Insert:” As used herein, “kinase insert” refers a stretch of up to about one hundred amino acid residues which divides the tyrosine kinase domain of certain tyrosine kinases in two. For human FLGK and FLGK, the kinase insert is located between helices αD and αE (FIGS. 1 and 3), contains autophosphorylation sites Tyr-583 and Tyr-585, and is characterized by at least amino acid residues 575 to 596 (FIG. 3).

[0032] “Unit Cell:” As used herein, “unit cell” refers to the smallest and simplest volume element (i.e., parallelpiped-shaped block) of a crystal that is completely representative of the unit of pattern of the crystal. The dimensions of the unit cell are defined by six numbers: dimensions a, b and c and angles α, β and γ (Blundel et al., 1976). A crystal is an efficiently packed array of many unit cells.

[0033] “Monoclinic Unit Cell:” As used herein, “monoclinic unit cell” refers to a unit cell wherein a≠b≠c; α=γ=90°; and β>90°.

[0034] “Crystal Lattice:” As used herein, “crystal lattice” refers to the array of points defined by the vertices of packed unit cells.

[0035] “Space Group:” As used herein, “space group” refers to the symmetry of a unit cell. In a space group designation (e.g., C2) the capital letter indicates the lattice type and the other symbols represent symmetry operations that can be carried out on the unit cell without changing its appearance.

[0036] “Asymmetric Unit:” As used herein, “asymmetric unit” refers to the largest aggregate of molecules in the unit cell that possesses no symmetry elements, but that can be juxtaposed on other identical entities by symmetry operations.

[0037] “Crystallographicallv-Related Dimer:” As used herein, “crystallographically-related dimer” refers to a dimer of two molecules wherein the symmetry axes or planes that relate the two molecules comprising the dimer coincide with the symmetry axes or planes of the crystal lattice.

[0038] “Non-Crystallographicallv-Related Dimer:” As used herein, “non-crystallographically-related dimer” refers to a dimer of two molecules wherein the symmetry axes or planes that relate the two molecules comprising the dimer do not coincide with the symmetry axes or, planes of the crystal lattice.

[0039] “Isomorphous Replacement:” As used herein, “isomorphous replacement” refers to the method of using heavy-atom derivative crystals to obtain the phase information necessary to elucidate the three-dimensional structure of a native crystal (Blundel et al., 1976). The phrase “heavy-atom derivatization” is synonymous with “isomorphous replacement.”

[0040] “Molecular Replacement:” As used herein, “molecular replacement” refers to the method of calculating initial phases for a new crystal whose structure coordinates are unknown by orienting and positioning a molecule whose structure coordinates are known within the unit cell of the new crystal so as to best account for the observed diffraction pattern of the new crystal. Phases are then calculated from this model and combined with observed amplitudes to provide an approximate Fourier synthesis of the structure of the molecules comprising the new crystal. This, in turn, is subject to any of several methods of refinement to provide a final, accurate set of structure coordinates for the new crystal (Lattman, 1985; Rossman, 1972).

3.2 Abbreviations

[0041] The amino acid notations used herein for the twenty genetically encoded L-amino acids are conventional and are as follows: One-Letter Three-Letter Amino Acid Symbol Symbol Alanine A Ala Arginine R Arg Asparagine N Asn Aspartic acid D Asp Cysteine C Cys Glutamine Q Gln Glutamic acid E Glu Glycine G Gly Histidine H His Isoleucine I Ile Leucine L Leu Lysine K Lys Methionine M Met Phenylalanine F Phe Proline P Pro Serine S Ser Threonine T Thr Tryptophan W Trp Tyrosine Y Tyr Valine V Val

4. BRIEF DESCRIPTION OF THE FIGURES

[0042]FIG. 1 provides a ribbon diagram of the structure of FLGK showing the side chains of tyrosines Tyr-653 and Tyr-654 and the α helical (αC, αD, αE, αEF, αF-αI), β strand (β1-β5, β7, β8), nucleotide-binding loop, catalytic loop, activation loop and kinase insert regions of the molecule. The termini are denoted by N and C. The loop between β2 and β3 is disordered, indicated by a break in the chain in this region.

[0043]FIG. 2 provides a stereo view of a C_(α) trace of FLGK shown in the same orientation as FIG. 1, with every tenth amino acid residue marked with a filled circle and every twentieth amino acid residue labeled with a residue number.

[0044]FIG. 3 provides a structure-based sequence alignment of human fibroblast growth factor receptor 1 (FGFR1), human fibroblast growth factor receptor 2 (FGFR2), human fibroblast growth factor receptor 3 (FGFR3), human fibroblast growth factor receptor 4 (FGFR4), a D. malanogaster homolog (DFGFR1), a C. elegans homolog (EGL-15) and insulin receptor tyrosine kinase (IRK).

[0045]FIGS. 4A and 4B provide ribbon diagrams of the N-terminal lobes (4A) and C-terminal lobes (4B) of FLGK and IRK in which the C_(α) atoms of the β sheets (4A) or α-helices (4B) of the two proteins have been superimposed.

[0046]FIG. 5 illustrates the side-chain positions of the tyrosine autophosphorylation sites of FLGK on the backbone representation of FLGK.

[0047]FIGS. 6A and. 6B are amino acid sequence alignments of the catalytic domains of PTKs, including receptor and non-receptor type PTKS. FIG. 6A depicts one representative member from each of the eighteen subfamilies of receptor tyrosine kinases. FIG. 6B depicts one representative member from each of the subfamilies of cytoplasmic tyrosine kinases. In FIGS. 6A and 6B highly conserved residues are boxed. The position of the glycine-rich domain, kinase insert, catalytic loop, and activation loop are indicated. The numbering is for human FGF-receptor.

4.1. BRIEF DESCRIPTION OF THE TABLES

[0048] Table 1 summarizes the X-ray crystallography data sets of FLGK derivative crystals :that were used to determine the structures of crystalline FLGK and crystalline FLGK:AMP-PCP co-complex of the invention;

[0049] Table 2 summarizes the X-ray crystallography refinement parameters of the structures of crystalline FLGK and crystalline FLGK:AMP-PCP co-complex of the invention;

[0050] Table 3 provides the atomic structure coordinates of native FLGK crystals of the invention as determined by X-ray crystallography; and

[0051] Table 4 provides the atomic structure coordinates of FLGK:AMP-PCP co-crystals of the invention as determined by X-ray crystallography.

5. DETAILED DESCRIPTION OF THE INVENTION

[0052] The present invention relates to crystalline polypeptides corresponding to the catalytic domain of receptor tyrosine kinases of the non-insulin receptor type. Such tyrosine kinases include receptors of a class that are not covalently cross-linked but are understood to undergo ligand-induced dimerization, as well as cytoplasmic tyrosine kinases. Preferably, the crystalline catalytic domains are of sufficient quality to allow for the determination of the three-dimensional X-ray diffraction structure to a resolution of about 1.5 Å to about 2.5 Å. The invention also relates to methods for preparing and crystallizing the polypeptides. The polypeptides themselves, as well as information derived from their crystal structures can be used to analyze and modify tyrosine kinase activity as well as to identify compounds that interact with the catalytic domain.

[0053] The polypeptides of the invention are designed on the basis of the structure of a region in the cytoplasmic domain of the receptor tyrosine kinase that contains the catalytic domain. By way of illustration, FIG. 6A shows the amino acid sequence alignment of the catalytic domains of eighteen human receptor tyrosine kinases; one representative member from each of the eighteen subfamilies is shown. FIG. 6B shows the alignment for cytoplasmic kinases. The applicants have discovered and determined the boundaries of the domain required for crystallization of the resulting polypeptide. Surprisingly, these boundaries differ from that required for catalytic activity. For example, referring to FIG. 6A, the domain required for catalytic activity is generally believed to span about 7 amino acid residues upstream of the first glycine (FIG. 6A residue number 485) of the N-terminal glycine-rich region through about 10 residues beyond the C-terminal conserved arginine (FIG. 6A, residue number 744). However, the Applicants have found that additional sequence upstream of the N-terminal glycine-rich region and downstream of the C-terminal conserved arginine are required for crystallization. In particular, the Applicants have determined that at least about 20 amino acid residues (+/−5 amino acid residues) upstream of the first glycine (i.e., FIG. 6A, residue number 485) in the conserved glycine-rich region of the catalytic domain, and at least about 17 amino acid residues (+/−5 amino acid residues) downstream of the conserved arginine (i.e., FIG. 6A, residue number 744) located at the C-terminal boundary of the catalytic domain are required to engineer a polypeptide suitable for crystallization.

[0054] In those situations where the resulting polypeptide contains cysteine residues that interfere with crystallization (e.g., cysteine residue numbers 488 and 584 in the FGF-R1 sequence shown in FIG. 6A), such cysteine residues can be substituted with an appropriate amino acid that does not readily form covalent bonds with other amino acid residues under crystallization conditions; e.g., by substituting the cysteine with Ala, Ser or Gly. Any cysteine located in a non-helical or non-β-stranded segment, based on secondary structure assignments, are good candidates for replacement. For example, cysteines located in regions corresponding to the glycine-rich-loop, the kinase insert, the juxtamembrane region or the activation loop are prime candidates for replacement. However, substitutions of cysteine residues that are conserved among the kinases (e.g., FIG. 6A at positions 725 and 736) are preferably avoided.

5.1 Crystalline Tyrosine Kinases

[0055] The crystals of the invention include native crystals, derivative crystals and co-crystals. The native crystals of the invention generally comprise substantially pure polypeptides corresponding to the tyrosine kinase domain in crystalline form.

[0056] It is to be understood that the crystalline tyrosine kinase domains of the invention are not limited to naturally occurring or native tyrosine kinase domains. Indeed, the crystals of the invention include mutants of native tyrosine kinase domains. Mutants of native tyrosine kinase domains are obtained by replacing at least one amino acid residue in a native tyrosine kinase domain with a different amino acid residue, or by adding or deleting amino acid residues within the native polypeptide or at the N- or C-terminus of the native polypeptide, and have substantially the same three-dimensional structure as the native tyrosine kinase domain from which the mutant is derived.

[0057] By having substantially the same three-dimensional structure is meant having a set of atomic structure coordinates that have a root mean square deviation of less than or equal to about 2 Å when superimposed with the atomic structure coordinates of the native tyrosine kinase domain from which the mutant is derived when at least about 50% to 100% of the C_(α) atoms of the native tyrosine kinase domain are included in the superposition.

[0058] Amino acid substitutions, deletions and additions which do not significantly interfere with the three-dimensional structure of the tyrosine kinase domain will depend, in part, on the region of the tyrosine kinase domain where the substitution, addition or deletion occurs. In highly variable regions of the molecule, such as those shown in FIG. 6, non-conservative substitutions as well as conservative substitutions may be tolerated without significantly disrupting the three-dimensional structure of the molecule. In highly conserved regions, or regions containing significant secondary structure, such as those regions shown in FIG. 6, conservative amino acid substitutions are preferred.

[0059] Conservative amino acid substitutions are well-known in the art, and include substitutions made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity and/or the amphipathic nature of the amino acid residues involved. For example, negatively charged amino acids include aspartic acid and glutamic acid; positively charged amino acids include lysine and arginine; amino acids with uncharged polar head groups having similar hydrophilicity values include the following: leucine, isoleucine, valine; glycine, alanine; asparagine, glutamine; serine, threonine; phenylalanine, tyrosine. Other conservative amino acid substitutions are well known in the art.

[0060] Of course, it is to be understood that for tyrosine kinase domains obtained in whole or in part by chemical synthesis, the selection of amino acids available for substitution or addition is not limited to the genetically encoded amino acids. Indeed, the mutants described herein may contain non-genetically encoded amino acids. Conservative amino acid substitutions for many of the commonly known non-genetically encoded amino acids are well known in the art. Conservative substitutions for other amino acids can be determined based on their physical properties as compared to the properties of the genetically encoded amino acids.

[0061] In some instances, it may be particularly advantageous or convenient to substitute, delete and/or add amino acid residues to a native tyrosine kinase domain in order to provide convenient cloning sites in cDNA encoding the polypeptide, to aid in purification of the polypeptide, etc. Such substitutions, deletions and/or additions which do not substantially alter the three dimensional structure of the native tyrosine kinase domain will be apparent to those having skills in the art.

[0062] It should be noted that the mutants contemplated herein need not exhibit PTK activity. Indeed, amino acid substitutions, additions or deletions that interfere with the kinase activity of the tyrosine kinase domain but which do not significantly alter the three-dimensional structure of the domain are specifically contemplated by the invention. Such crystalline polypeptides, or the atomic structure coordinates obtained therefrom, can be used to identify compounds that bind to the native domain. These compounds may affect the activity or the native domain.

[0063] The derivative crystals of the invention generally comprise a crystalline tyrosine kinase domain polypeptide in covalent association with one or more heavy metal atoms. The polypeptide may correspond to a native or a mutated tyrosine kinase domain. Heavy metal atoms useful for providing derivative crystals include, by way of example and not limitation, gold, mercury, etc.

[0064] The co-crystals of the invention generally comprise a crystalline tyrosine kinase domain polypeptide in association with one or more compounds. The association may be covalent or non-covalent. Such compounds include, but are not limited to, cofactors, substrates, substrate analogues, inhibitors, allosteric effectors, etc.

5.2 Production of Polypeptides

[0065] The native and mutated tyrosine kinase domain polypeptides described herein may be chemically synthesized in whole or part using techniques that are well-known in the art (see, e.g., Creighton, 1983). Alternatively, methods which are well known to those skilled in the art can be used to construct expression vectors containing the native or mutated tyrosine kinase domain polypeptide coding sequence and appropriate transcriptional/translational control signals. These methods include in vitro recombinant DNA techniques, synthetic techniques and in vivo recombination/genetic recombination. See, for example, the techniques described in Maniatis et al., 1989 and Ausubel et al., 1989.

[0066] A variety of host-expression vector systems may be utilized to express the tyrosine kinase domain coding sequence. These include but are not limited to microorganisms such as bacteria transformed with recombinant bacteriophage DNA, plasmid DNA or cosmid DNA expression vectors containing the tyrosine kinase domain coding sequence; yeast transformed with recombinant yeast expression vectors containing the tyrosine kinase domain coding sequence; insect cell systems infected with recombinant virus expression vectors (e.g., baculovirus) containing the tyrosine kinase domain coding sequence; plant cell systems infected with recombinant virus expression vectors (e.g., cauliflower mosaic virus, CaMV; tobacco mosaic virus, TMV) or transformed with recombinant plasmid expression vectors (e.g., Ti plasmid) containing the tyrosine kinase domain coding sequence; or animal cell systems. The expression elements of these systems vary in their strength and specificities. Depending on the host/vector system utilized, any of a number of suitable transcription and translation elements, including constitutive and inducible promoters, may be used in the expression vector. For example, when cloning in bacterial systems, inducible promoters such as pL of bacteriophage λ, plac, ptrp, ptac (ptrp-lac hybrid promoter) and the like may be used; when cloning in insect cell systems, promoters such as the baculov-rus polyhedrin promoter may be used.; when cloning in plant cell systems, promoters derived from the genome of plant cells (e.g., heat shock promoters; the promoter for the small subunit of RUBISCO; the promoter for the chlorophyll a/b binding protein) or from plant viruses (e.g., the 35S RNA promoter of CaMV; the coat protein promoter of TMV) may be used; when cloning in mammalian cell systems, promoters derived from the genome of mammalian cells (e.g., metallothionein promoter) or from mammalian viruses (e.g., the adenovirus late promoter; the vaccinia virus 7.5K promoter) may be used; when generating cell lines that contain multiple copies of the tyrosine kinase domain DNA, SV40-, BPV- and EBV-based vectors may be used with an appropriate selectable marker.

5.3 Crystallization of Polypeptides and Characterization of Crystal Structure

[0067] The native, derivative and co-crystals of the invention can be obtained by conventional means as are well-known in the art of protein crystallography, including batch, liquid bridge, dialysis, vapor diffusion and hanging drop methods (see, e.q., McPherson, 1982; McPherson, 1990; Webber, 1991).

[0068] Generally, the native crystals of the invention are grown by dissolving substantially pure tyrosine kinase domain polypeptide in an aqueous buffer containing a precipitant at a concentration just below that necessary to precipitate the protein. Water is removed by controlled evaporation to produce precipitating conditions, which are maintained until crystal growth ceases.

[0069] In a preferred embodiment of the invention, native crystals are grown by vapor diffusion in hanging drops (McPherson, 1982 and 1990). In this method, the polypeptide/precipitant solution is allowed to equilibrate in a closed container with a larger aqueous reservoir having a precipitant concentration optimal for producing crystals. Generally, less than about 25 μL of substantially pure polypeptide solution is mixed with an equal volume of reservoir solution, giving a precipitant concentration about half that required for crystallization. This solution is suspended as a droplet underneath a coverslip, which is sealed onto the top of the reservoir. The sealed container is allowed to stand, usually for about 2-6 weeks, until crystals grow.

[0070] For crystals of the invention, it has been found that hanging drops containing about 2.0 μL of tyrosine kinase domain polypeptide (10 mg/mL in 10 mM Tris-HCl, pH 8.0, 10 mM NaCl and 2 mM dithiothreitol) and 2.0 μL reservoir solution (16% w/v polyethylene glycol MW 10000, 0.3 M (NH₄)₂SO₄, 5% v/v ethylene glycol or glycerol and 100 mM bis-Tris, pH 6.5) suspended over 0.5 mL reservoir buffer for about 3-4 weeks at 4° C. provide crystals suitable for high resolution X-ray structure determination.

[0071] Of course, those having skill in the art will recognize that the above-described crystallization conditions can be varied. Such variations may be used alone or in combination, and include polypeptide solutions containing polypeptide concentrations between 1 mg/mL and 60 mg/mL, Tris-HCl concentrations between 10 mM and 200 mM, dithiothreitol concentrations between 0 mM and 20 mM, pH ranges between 5.5 and 7.5; and reservoir solutions containing polyethylene glycol concentrations between 10% and 30% (w/v), polyethylene glycol molecular weights between 1000 and 20,000, (NH₄)₂SO₄ concentrations between 0.1 M and 0.5 M, ethylene glycol or glycerol concentrations between 0% and 20% (v/v), bis-Tris concentrations between 10 mM and 200 mM, pH ranges between 5.5 and 7.5 and temperature ranges between 0° C. and 25° C. Other buffer solutions may be used such as HEPES buffer, so long as the desired pH range is maintained.

[0072] Derivative crystals of the invention can be obtained by soaking native crystals in mother liquor containing salts of heavy metal atoms. It has been found that soaking a native crystal in a solution containing about 0.1 mM to about 5 mM. thimerosal, 4-chloromeruribenzoic acid or KAu(CN)₂ for about 2 hr to about 72 hr provides derivative crystals suitable for use as isomorphous replacements in determining the X-ray crystal structure of the tyrosine kinase domain polypeptide.

[0073] Co-crystals of the invention can be obtained by soaking a native crystal in mother liquor containing compound that bind the kinase domain, or described above, or can be obtained by co-crystallizing the kinase domain polypeptide in the presence of one or more binding compounds.

[0074] For co-crystals of tyrosine kinase domain polypeptide in co-complex with AMP-PCP, it has been found that co-crystallizing the kinase domain polypeptide in the presence of AMP-PCP using the above-described crystallization conditions for obtaining native crystals with a polypeptide solution additionally containing 10 mM AMP-PCP and 20 mM MgCl₂ yields co-crystals suitable for the high resolution structure determination by X-ray crystallography. Of course, those having skill in the art will recognize that the concentrations of AMP-PCP and MgCl₂ in the polypeptide solution can be varied, alone or in combination with the variations described above for native crystals. Such variations include polypeptide solutions containing AMP-PCP concentrations between 0.1 mM and 50 mM and MgCl₂ concentrations between 0 mM and 50 mM.

[0075] Methods for obtaining the three-dimensional structure of the crystalline tyrosine kinase domains described herein, as well as the atomic structure coordinates, are well-known in the art (see, e.g., Ducruix and Geige, 1992, and references cited therein).

5.4 Uses of the Crystals and Atomic Structure Coordinates

[0076] The crystals of the invention, and particularly the atomic structure coordinates obtained therefrom, have a wide variety of uses. For example, the crystals described herein can be used as a starting material in any of the art-known methods of use for receptor and non-receptor tyrosine kinases. Such methods of use include, for example, identifying molecules that bind to the native or mutated catalytic domain of tyrosine kinases. The crystals and structure coordinates are particularly-useful for identifying compounds that inhibit receptor and non-receptor tyrosine kinases as an approach towards developing new therapeutic agents (see, e.g., Levitzki and Gazit, 1995).

[0077] The structure coordinates described herein can be used as phasing models in determining the crystal structures of additional native or mutated tyrosine kinase domains, as well as the structures of co-crystals of such domains with ligands such as inhibitors, agonists, antagonists, etc. The structure coordinates, as well as models of the three-dimensional structures obtained-therefrom, can also be used to aid the elucidation of solution-based structures of native or mutated tyrosine kinase domains, such as those obtained via NMR. Thus, the crystals and atomic structure coordinates of the invention provide a convenient means for elucidating the structures and functions of receptor and non-receptor tyrosine kinases.

[0078] For purposes of clarity and discussion, the crystals of the invention will be described by reference to specific FLGK exemplary crystals. Those skilled in the art will appreciate that the principles described herein are generally applicable to crystals of the tyrosine kinase domain of any cytoplasmic tyrosine kinase that undergoes ligand-induced dimerization or receptor tyrosine kinase, including but not limited to the tyrosine kinases of FIG. 6.

5.5 Crystalline FLGK

[0079] In one illustrative embodiment, the invention provides crystals of FLGK. The crystals were obtained by the methods provided in the Examples. The FLGK crystals, which may be native crystals, derivative crystals or co-crystals, have monoclinic unit cells (i.e., unit cells wherein a≠b≠c; α=γ=90°; and β>90°) and space group symmetry C2. There are two FLGK molecules in the asymmetric unit, related by an approximate two-fold axis.

[0080] Two forms of crystalline FLGK were obtained. In one form (designated “C2-A form”), the unit cell has dimensions of a=208.3+/−0.2 Å, b=57.8+/−0.2 Å, c=65.5+/−0.2 Å and β=107.2°+/−0.2°. In another form (designated “C2-B form!”), the unit cell has dimensions of a=211.6+/−0.2 Å, b=51.3+/−0.2 Å, c=66.1+/−0.2 Å and β=107.70+/−0.2°.

[0081] Three distinct two-fold related FLGK dimers are observed in both the C2-A and C2-B forms of the FLGK crystal, one non-crystallographically related dimer and two crystallographically related dimers. The non-crystallographically related dimer comprises the two molecules in the asymmetric unit. The residues making up the dimer interface are located in C-terminal lobe. In this dimer, the C-terminal lobes abut with the N-terminal lobes distal to one another. The total amount of surface area buried in the surface is about 950 Å². Very few of the interactions in the interface are of a specific nature, e.g., hydrogen-bonding or close packing of hydrophobic residues.

[0082] There are two crystallographically-related dimers in the C2 lattice. In the first dimer, the residues that constitute the dimer interface are limited to those in the β-sheet of the N-terminal lobe (amino acid residues 477, 479, 498, 506, 508 and 496). The total surface area buried in this interface is about 670 Å². The interactions are rather specific. Three hydrophobic residues which are partially solvent-exposed in the monomer, Val-479, Ile-498 and Val-508, come together with their two-fold-related residues to form a compact hydrophobic plug. This plug is capped on either side by a salt bridge between Arg-477 and Glu-496. In addition, two main-chain hydrogen-bonds connect the β-sheets of the two monomers at the start of β3 (amino acid residues 506 and 508). The residues in this dimer interface, or their residue character, are generally conserved in the mammalian FGF receptors, but not in the invertebrate homologues.

[0083] The other crystallographically-related dimer buries about 1650 Å² in its interface. In this dimer, the αC helices of the two monomers are nearly parallel and contact each other at their C-terminal ends. Met-534 and Met-537 are in van der Waals contact with their two-fold-related residues. Other hydrophobic contacts involve Pro-466 with Ile-648 and Pro-469 with Ile-676 and Thr-678. In addition, hydrogen bonds (side-chain to main-chain) are made between Arg-470 and Lys-618 and between His-649 and Glu-464, and there are several water molecules that bridge the two monomers through hydrogen bonding.

[0084] In the C2-B form of the crystal, the monomers of this second crystallographically-related dimer are shifted slightly with respect to one another (6° rotation), indicating that this interface is somewhat fluid.

[0085] In both of the crystallographically-related dimers, the N-termini of the two molecules comprising the dimer point in the same direction and are reasonably close to one another.

[0086] 5.5.1 Structures of FLGK and FLGK:AMP-PCP Co-Complex

[0087] The-present invention also provides, for the first time, the high-resolution three-dimensional structures and atomic structure coordinates of crystalline FLGK and crystalline FLGK:AMP-PCP co-complex as determined by X-ray crystallography. The specific methods used to obtain the structure coordinates are provided in the examples. The atomic structure coordinates of crystalline FLGK, obtained from the C2-A form of the crystal to 2.0 Å resolution, are listed in Table 3; the coordinates of crystalline FLGK:AMP-PCP co-complex, obtained from the C2-A form of the crystal to 2.3 Å resolution are listed in Table 4.

[0088] Those having skill in the art will recognize that atomic structure coordinates as determined by X-ray crystallography are not without error. Thus, it is to be understood that any set of structure coordinates obtained for crystals of FLGK, whether native crystals, derivative crystals or co-crystals, that have a root mean square deviation (“r.m.s.d.”) of less than or equal to about 1.5 Å when superimposed, using backbone atoms (N, C_(α), C and O), on the structure coordinates listed in Table 3 or Table 4 are considered to be identical with the structure coordinates listed in the Tables when at least about 50% to 100% of the backbone atoms of FLGK are included in the superposition.

[0089] Referring now to FIG. 1, the overall structure of FLGK is bi-lobate. The N-terminal lobe of FLGK spans amino acid residues 456-567 (FIG. 3) and comprises a curled β-sheet of five anti-parallel strands (β1-β5) and one α-helix (αC). The C-terminal lobe spans amino acid residues 568-765 (FIG. 3) and comprises two β-strands (β7, β8) and seven α-helices (αD, αE, αEF, αF-αI). The secondary structure nomenclature follows that used for IRK (Hubbard et al., 1994) which in turn is based on the assignments for cAPK (Knighton et al., 1991). FIG. 2 shows a stereo view of a C_(α) trace of FLGK in the same orientation as FIG. 1.

[0090] A structure-based sequence alignment of the tyrosine kinase domains of human fibroblast growth factor receptor 1 (human FLGK; labelled FGFR1), human fibroblast growth factor receptors 2, 3 and 4 (labelled FGFR2, FGFR3 and FGFR4, respectively), a.D. melanogaster homologue (labelled DFDFR1), a C elegans homologue (labelled EGL-15) and insulin receptor kinase (labelled IRK), is shown in FIG. 3. The sequence of FLGK, which is not shown in FIG. 3 is identical to the sequence of FGFR1 except that FLGK has the following amino acid substitutions and additions: Cys-488→Ala, Cys-584→Ser, Leu-457→Val and an additional five N-terminal amino acids (Ser-Ala-Ala-Gly-Thr). The secondary structure assignments for FGFR1 and IRK were obtained using the Kabsch and Sander algorithm (Kabsch and Sander, 1983) as implemented in PROCHECK (Laskowski et al., 1993). In the FGF receptor sequences, a period represents sequence identity to FGFR1. In the IRK sequence, residues that are identical to FGFR1 are highlighted. A hyphen denotes an insertion.

[0091] The numbers under the EGL-15 sequence represent the fractional solvent accessibility (FSA2) of the residue in the FLGK structure. The FSA ratio is the ratio of the solvent-accessible surface area of a residue in a Gly-X-Gly tripeptide compared to that in the FLGK structure. A value of 0 represents an FSA between 0.00 and 0.09; 1 represents an FSA between 0.10 and 0.19, etc. The higher the value, the more solvent-exposed the residue. An asterisk or pound sign in the FSA line indicates that the residue (asterisk) or side chain (pound sign) is not included in the atom model due to disorder. The numbers below the FSA line are the FSAs for those residues that form part of a dimer interface.

[0092] The amino acid residue numbers for FGFR1, and hence FLGK, and IRK provided in FIG. 3 are used in the discussion that follows. Significant differences in the N-terminal lobe of FLGK as compared to IRK are found in the loops between β0 strands and in αC. Residues from the end of β1 through the beginning of β2 (amino acid residues 485-490) form the nucleotide-binding loop, named because of its role in ATP coordination. This residue stretch contains the protein kinase-conserved GXGXXG sequence motif, where X is any amino acid. This loop is poorly ordered in one FLGK molecule in the asymmetric unit and disordered (i.e., not included in the atomic model) in the other FLGK molecule in the asymmetric unit. The loop between β1 and β3 is disordered in both FLGK molecules comprising the asymmetric unit.

[0093] Referring now to FIG. 4A, which provides a ribbon diagram of the N-terminal lobes of FLGK and IRK in which the C_(α) atoms of the β-sheets have been superimposed, it can be seen that in FLGK αC is longer by one helical turn than in IRK and is oriented such that residues Lys-514 and Glu-531, which are conserved in protein kinases, form a salt bridge (represented by a black line). While not intending to be bound by theory, this salt bridge is believed to be important for proper positioning of the conserved lysine side chain, which coordinates two phosphate oxygens of ATP. The salt bridge is observed in the structures of cAPK (Knighton et al., 1991) and mitogen-activated protein kinase (MAPK) (Zhang et al., 1994).

[0094] Referring now to FIG. 4B, which provides a ribbon diagram of the C-terminal lobes of FLGK and IRK in which the C_(α) atoms of the α-helices have been superimposed, a significant difference is found in the C-terminal helix of FLGK when compared to IRK; helix αI of FLGK is longer by seven residues (two helical turns) than its .counterpart in IRK. The extended length of αI is presumably important in the biological functioning of FGF receptors, since the tyrosine autophosphorylation site to which an SH2 domain of PLCγ binds is six residues C-terminal to this helix.

[0095] The structure of FLGK displays an open disposition of the N- and C-terminal lobes. Despite having different sets of lattice contacts, the two FLGK molecules in the asymmetric unit have only a 2° difference in relative lobe orientation. It appears as though the stearic interaction between residues in αC (Glu-531 and Met-534) with Phe-642 and Gly-643 of the protein kinase-conserved DFG sequence-at the beginning of the activation loop accounts for the open conformation of FLGK.

[0096] The active site of FLGK is characterized by at least amino acid residues spanning the catalytic loop, activation loop and nucleotide binding loop. Unlike the structure of IRK, in which Tyr-1162 occupies the active site of the molecule, the active sites of both FLGK molecules in the asymmetric unit are unoccupied.

[0097] The activation loop, which regulates phosphorylationl is characterized by at least resides 640 to 663. Quite surprisingly, while the activation loops of FLGK and IRK contain the same number of amino acid residues and share greater than 50% sequence homology, the paths of the polypeptide chains are strikingly dissimilar, diverging at Ala-640 (Gly-1149 in IRK) and reconverging at Val-664 (Val-1173 in IRK). Tyr-653 and Tyr 564 are not bound in the active site. Instead, these residues point away from it. Tyr-653 is in van der Waals contact with several hydrophobic residues (Val-664, Leu-672 and Phe-710) and is hydrogen-bonded via its hydroxyl group to a backbone carbonyl oxygen (Leu-672). Tyr-654 is more solvent exposed than Tyr-653, and its only van der Waals contact is with Val-706. Temperature factor data suggest that the activation loop is relatively mobile and adopts multiple conformations.

[0098] The catalytic loop of protein kinases lies between secondary structure elements αE and β7 and contains an invariant aspartic acid residue (Asp-623 in FLGK) which serves as the catalytic base in the phosphotransfer reaction, abstracting the proton from the hydroxyl group of the substrate tyrosine, serine or threonine. The catalytic loop sequence of FLGK comprises at least residues His-621 to Asn-628 (amino acid sequence HRDLAARN), and is identical to that for IRK and most receptor and non-receptor PTKs.

[0099] In addition to the two tyrosine autophosphorylation sites in the activation loop (Tyr-653 and Tyr-654), there are four other autophosphorylation sites present in the FLGK crystals of the invention: one in the juxtamembrane region (Tyr-463), two in the kinase insert (Tyr-583 and Tyr-585) and one in the C-terminal lobe (Tyr-730) (Mohammadi et al., 1996). They exhibit varying degrees of conservation in mammalian FGF receptors: Tyr-463 and Tyr-585 in FGFR1 and 2; Tyr-583 in FGFR1, 2 and 3; and Tyr-730 in FGFR 1, 2, 3 and 4 (FIG. 3).

[0100] Referring now to FIG. 5, the positions of the autophosphorylation sites are mapped onto the FLGK structure. The juxtamembrane site (Tyr-463) and the residues N-terminal to it are disordered in one of the FLGK molecules in the asymmetric unit. In the other molecule in the asymmetric unit Tyr-463 is involved in a lattice contact.

[0101] The kinase insert region (the region between helices αD and αE) contains autophosphorylation sites Tyr-583 and Tyr-585 and is disordered in both FLGK molecules in the asymmetric unit of the C2-A form of the crystal. In the C2-B form, several lattice contacts partially pin down this region in one of the two FLGK molecules in the-asymmetric unit, allowing a trace of the polypeptide chain to be made. There is no well-defined secondary structure for these residues. Tyr-730, situated in αH in the C-terminal lobe, is nearly buried and the side-chain hydroxyl group makes two hydrogen-bonds. The side chains of neighboring Met-732 and Met-733 are both buried. Therefore, phosphorylation of Tyr-730 would presumably require prior unfolding of αH.

[0102] Aside from Tyr-730, the five other autophosphorylation sites (including Tyr-653 and Tyr-654) are found in relatively mobile segments of the FLGK molecule. While not intending to be bound by theory, the spatial positions of the autophosphorylation sites relative to the active site suggest that autophosphorylation occurs by a trans mechanism between two kinase domains, supporting the hypothesis that ligand-induced receptor dimerization is critical for the initiation of autophosphorylation events.

[0103] The structure of crystalline FLGK:AMP-PCP co-complex is essentially similar to that observed for crystalline FLGK. There are no significant changes in the structure of FLGK induced by AMP-PCP binding. In particular, binding of AMP-PCP, and by extension ATP, does not by itself promote lobe closure under the crystallization conditions used. Furthermore, complexation did not result in any noticeable changes in the conformations of the activation and nucleotide-binding loops.

[0104] The crystalline FLGK:AMP-PCP co-complex contains hydrogen bonds that are present between N1 of adenine and the amide nitrogen of Ala-564 and between N6 of adenine and the carbonyl oxygen of Glu-562. The adenine ring is flanked on one side by Leu-484 and Val-492 (N-terminal lobe) and on the other side by Leu-630 (C-terminal lobe). The ribose hydroxyl groups make no direct hydrogen bonds with protein atoms. Lys-514 is hydrogen-bonded to oxygens of the β- and γ-phosphates. There is no unambiguous electron density that would indicate the positions of Mg²⁺ ions. Generally, AMP-PCP appears to be coordinated rather loosely to unphosphorylated FLGK, being bound to the “roof” of the cleft rather than being tightly sandwiched between the two kinase lobes.

[0105] 5.5.2 Structural Differences Between FGF-R and IRK

[0106] Several features distinguish the FGF-receptor structure from that of the insulin-receptor tyrosine kinase. These distinctions are likely to be important in signalling by FGF-receptors, and other monomeric receptors that are believed to undergo ligand-induced dimerization.

[0107] The most significant difference between the structures of FGFR1K and IRK is the conformation of the activation loop. In FGFR1K, the activation loop is disposed such that the binding site for substrate peptides is blocked not by an activation loop tyrosine, as in IRK, but by Arg-661 and PTK-invariant Pro-663, while the ATP binding site is accessible. This represents another molecular mechanism by which a receptor PTK may be autoinhibited. The observed autoinhibition in FGFR1K would appear to be weaker than that in IRK because of fewer specific interactions made by residues in the FGFR1K activation loop (manifested in the relatively higher B-values) and the accessibility of the ATP site. One obvious distinction between the insulin and FGF receptor families is that in the former, receptors are covalently linked heterotetramers (α₂β₂), whereas in the latter, receptor dimerization is ligand dependent. Receptors whose kinase domains are always in close proximity may require a stronger autoinhibition mechanism than those receptors that associate only upon ligand binding (Taylor et al., 1995). Since most growth factor receptors undergo ligand-dependent dimerization and activation, the FGF receptor autoinhibition mechanism appears to be a more general one.

6. EXAMPLE Preparation of Crystals of The Catalytic Domain of the FGF-R-1

[0108] The subsections below describe the production of a polypeptide containing the catalytic domain of the FGF-receptor-1, and the preparation and characterization of crystals, derivative crystals and co-crystals of sufficient quality for X-ray diffraction analysis.

6.1 Production and Purification of FLGK

[0109] A recombinant baculovirus (Pharmingen, Calif.) was engineered to encode the protein of. SEQ ID NO:3. Compared to the sequence of human FLGK (SEQ ID NO:1), the protein of SEQ ID NO:3 has a cleavable-histidine tag (MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDTSSR) fused to the N-terminus to aid in protein purification. Also, three amino acid substitutions were introduced: Cys-488ΔAla, Cys-584→Ser and Leu→457→Val. The two cysteine substitutions were made to prevent the formation of disulfide-linked oligomers, which occurs for the native protein. The substitution Leu→457→Val was necessary to introduce a NcoI cloning site near Met-456. The codon for Tyr-766 (TAC) was changed to a stop codon (TAG) and a HindIII-cloning site was generated following this stop codon. These substitutions were introduced into the full length cDNA of human FLGK (SEQ ID NO:4) in m13MP19 by site-directed mutagenesis using an in vitro mutagenesis kit according to the manufacturer's protocol (Amersham). The resulting construct was digested with NcoI and HindIII and was ligated into appropriately digested pBlueBac HistagB (Invitrogen). Transfection of insect cells (Sf9) was performed with the BaculoGold transfection system according to the manufacturer's protocol (Pharmingen). Following identification of positive plaques, the recombinant baculovirus was amplified to high titer (5×10⁷ virus particles/ml). Sf9 cells were grown in 175-cm² flasks to a density of 2−3×10⁷ per flask and infected with recombinant baculovirus with a multiplicity of infection (MOI) of ten (10). After 48 hrs., cells were harvested by centrifugation at 3,000 g for 35 min. at 4° C. and then lysed in lysis buffer (25 mM HEPES, pH 7.5, 150 mM NaCl, 10% glycerol, 1.5 MM MgCl₂, 1% Triton X-100, 10 μg/ml aprotonin, 10 μg/ml leupeptin and 1 mM phenylmethylsulfonyl fluoride (PMSF)). Lysates were centrifuged in a Sorval RC 5C centrifuge (Dupont) for 1 hr at 4° C. at 40,000 g followed by ultracentrifugation in an XL-80 ultracentrifuge (Beckman) at 100,000 g for 1 hr. After centrifugation, the clarified lysate was passed over a Ni²⁺-chelating column (Pharmacia), and the bound histidine-tagged fusion protein was eluted with 100 mM imidazole (pH 7.5). Pooled fractions were loaded onto a Mono Q anion exchange column (Pharmacia) and eluted with a NaCl gradient from 0 to 500 mM. The fractions containing the fusion protein were concentrated in a Centricon-30 (Amicon), and the histidine tag was removed by overnight digestion with enterokinase (Biozyme) at 20° C. The digestion was terminated by the addition of aprotonin, leupeptin, PMSF, TPCK (tosyl-L-phenylalanine chloromethyl ketone) and bovine pancreatic trypsin inhibitor (BPTI). The cleaved kinase domain was then separated from the histidine tag on a Superose 12 size-exclusion column (Pharmacia). The eluted kinase domain was further purified on a Mono Q column. The purified kinase domain was analyzed by N-terminal sequencing and mass spectrometry. Five amino acids (SAAGT) remained from the histidine tag. The predicted molecular mass was confirmed by mass spectrometry. The amino acid sequence of the purified protein (FLGK) is provided in SEQ ID NO:2.

[0110]6.1.1 Preparation of FLGK Native Crystals

[0111] FLGK native crystals (C2-A form) were grown at 4° C. by vapor diffusion in hanging drops (McPherson, 1990). 2 μL FLGK (SEQ ID NO:2) (20-mg/mL in 10 mM Tris-HCl, 10 mM NaCl, 2 mM DTT, pH 8.0) was mixed with an equal volume (2 μL) of reservoir buffer (16% w/v polyethylene glycol MW 10,000, 0.3 M (NH₄)₂SO₄, 5% v/v ethylene glycol, 100 mM bis-Tris, pH 6.5) and allowed to stand over 0.5 ml reservoir solution at 4° C. Irregular crystals typically grew to 0.6×0.3×0.2 mm over a period of 3-4 weeks. The solvent content of the crystal was 55% (assuming a partial specific volume of 0.73 cm³/gm).

[0112] FLGK native crystals (C2-B form) were grown as described above using a reservoir buffer containing 5% v/v glycerol instead of ethylene glycol. The solvent content of the crystal was 50% (assuming a partial specific volume of 0.73 cm³/gm).

[0113] 6.1.2 Preparation of Heavy Atom Derivative Crystals

[0114] Heavy atom derivative crystals were obtained by soaking FLGK native crystals (C2-A form) in a solution containing ethylmercurithiosalicylic acid (thimerosal), KAu.(CN)₂ or 4-chloromercuribenzoic acid, as provided in Table 1, infra, and containing 25% PEG 10000, 0.3M (NH₄)₂SO₄, 5% ethylene glycol or glycerol, and 100 mM bis-Tris (pH 6.5), and were flash-cooled either in liquid nitrogen directly (Synchrotron) or in a dry nitrogen stream at −175° C. (rotating anode).

[0115] 6.1.3 Preparation of FLGK:AMP-PCP Co-Crystals

[0116] Crystals of FLGK complexed with AMP-PCP were obtained as described in Example 6.1.1, except that the protein solution additionally contained 10 mM AMP-PCP and 20 mM MgCl₂.

6.2 Analysis and Characterization of FLGK Crystals

[0117] 6.2.1 Diffraction Data Collection

[0118] Data were collected either on a Rigaku RU-200 rotating anode operated at 50 kV and 100 mA (Cu Ka) and equipped with double-focusing mirrors and an R-AXIS IIC image plate detector, or at beamline X-4 Å at the National Synchrotron Light Source, Brookhaven National Laboratory. Synchrotron data (λ=1.07 Å) were collected on Fuji image plates and read with a Fuji scanner. One cryo-cooled crystal was used for each of the data sets. To obtain cryo-cooled crystals, crystals were soaked in a cryo-protectant solution containing 25% PEG 10000, 0.3 M (NH₄)₂SO₄, 5% ethylene glycol or glycerol and 100 mM bis-Tris (pH 6.5), and were flash-cooled either in liquid nitrogen directly (synchrotron data) or in a dry nitrogen stream at −175° C. (rotating anode data). All data were processed using DENZO and SCALEPACK (Otwinowski, 1993).

[0119] 6.2.2 Structure Determination

[0120] A molecular replacement solution was found initially for the C2-B crystal form using an IRK search model that consisted of polyalanine plus the common side chains for residues 993-1263 (FLGK residues 475-754), excluding residues 1094-1105 (kinase insert) and 1153-1170 (activation loop). With AMORE (Navaza, 1994), using 80% of the structure factor amplitudes between 15.0 and 3.5 Å, one of the two molecules in the asymmetric unit was located. The correlation coefficient (c.c.) for the correct 1-molecule solution was 0.23 (versus 0.20 for the highest incorrect solution). This molecule was rigid body-refined in X-PLOR (Brunger, 1992), first as one rigid body unit, then as two units each comprising a lobe of the kinase. Rigid body refinement (12.0-3.5 Å, F>3σ) resulted in a relative rotation of the two lobes of ˜10° and an increase of the c.c. from 0.20 to 0.25. The rigid body-refined molecule was then used as a new search model in AMORE, and this time both molecules in the asymmetric unit were located. The c.c. for the correct 2-molecule solution was 0.35 (versus 0.27 for the highest incorrect solution).

[0121] Multiple cycles of model-building and refinement against 6.0-2.4 Å data resulted in the addition to the model of many of the side chains and some of the missing polypeptide chain. Model building was performed using TOM/FRODO (Jones, 1985) and conjugate-gradient minimization and simulated annealing were performed using X-PLOR (Brunger, 1992). At this stage, the R-value was 30% (free R-value of 36%). To help expedite model building and refinement, experimental phases were obtained. Because crystals grown in the presence of ethylene glycol were easier to manipulate than those grown in glycerol, several heavy-atom derivative data sets were collected from C2-A crystals that had been soaked in various heavy atom solutions. The C2-B structure was subsequently refined against 6.0-2.4 Å data to an R-value of 23.8% (free R-value of 30.4%) with r.m.s.d. values of 0.008 Å for bond distances and 1.4° for bond angles.

[0122] Molecular replacement was used to locate the two FLGK molecules (designated FLGK-A and FLGK-B) in the asymmetric unit of the C2-A crystal form. Using AMORE with 80% of structure factor amplitudes between 15.0 and 3.5 Å and the C2-B model, the c.c. for the correct 2-molecule solution was 0.62 (versus 0.35 for the highest incorrect solution). Heavy atom positions were determined from difference Fourier maps using the calculated phases from the partial model. Refinement of heavy atom parameters and phase determination were performed with MLPHARE (Otwinowski, 1991). An initial molecular isomorphous replacement (MIR)-phased electron density map was calculated with data between 2.0. and 2.8 Å resolution. This map was improved by solvent flattening, histogram matching, and non-crystallographic symmetry (NCS) averaging using DM (Cowtan, 1994).

[0123] Refinement of the C2-A FLGK structure against 6.0-2.0 Å data proceeded by conjugate-gradient minimization and simulated annealing using X-PLOR. Tight NCS restraints were imposed until data to 2.0 Å resolution were included in the refinement, at which point the restraints were lifted. An overall anisotropic B-value was calculated using X-PLOR and applied to the observed structure factors, reducing the R-value by ˜3%. Water molecules whose B-values refined to ≧70 Å² were omitted from the subsequent refinement round. The average B-value is 37.5 Å² for all protein atoms, 35.4 Å² for protein atoms in FLGK-A, 39.7 Å² for protein atoms in FLGK-B, and 40.2 Å² for water molecules. The side chains for Cys-603 in FLGK-A and FLGK-B and for Met-534 in FLGK-B have been modeled in two different conformations. Residues that are not included in the atomic model due to poor supporting electron density are for FLGK-A: 456-463, 486-490, 501-504, 580-591, 763-765; and for FLG-B: 456-460, 501-504, 578-593, 646-651, 657-659, 762-765.

[0124] The positions of the two AMP-PCP molecules (one per FLGK molecule) were easily identified in 2F_(obs(co-complex))-F_(calc(flgk)) difference Fourier maps. The AMP-PCP molecule bound to FLGK-B is less tightly bound and has been modeled with an occupancy of 0.5.

[0125] The following table summarizes the X-ray crystallography data sets of FLGK derivative crystals that were used to determine the structures of crystalline FLGK and crystalline FLGK:AMP-PCP co-complex of the invention. TABLE 1 Data Collection and MIR Phasing Summary Native AMP-PCP Thi-1^(a) Thi-2^(a) PCMB^(a) KAu(CN)₂ X-ray source X-4A RU-200 RU-200 RU-200 RU-200 RU-200 Resolution limit (Å) 2.0 2.3 2.6 2.8 2.8 2.8 Number of sites — — 4 7 2 2 Conc. (mM)/time (h) — — 0.1/24 0.1/48 0.2/2 5.0/72 R_(sym) ^(b)(%) 4.8(19.7)^(c) 4.5(23.3)^(c) 5.5 9.8 6.8 6.8 Total observations 122569 91324 55456 59488 67988 45303 Unique reflections  50771 31997  42820^(d)  35538^(d) 18619 18202 Completeness (%) 97.3(96.3)^(c) 95.5(93.7)^(c) 95.0 96.7 98.0 97.7 Signal (% 1 > 3σ) 80.7(50.3)^(c) 79.6(51.7)^(c) 69.8 66.8 84.7 77.6 R_(iso) ^(e)(%) — — 17.1 31.2 15.4 15.2 Phasing power^(f) — — 1.8 2.0 1.0 0.9 R_(cullis) ^(g)(%) — — 0.55 0.50 0.81 0.84 Overall FOM^(h) 0.60

[0126] 6.2.3 Structure Analyses

[0127] Atomic superpositions were performed with TOSS is (Hendrickson, 1979). Per residue solvent accessible surface calculations were done with X-PLOR. The surface area buried in a dimer interface was calculated with GRASP (Nicholls et al., 1991) using a probe radius of 1.4 Å. The stereochemical quality of the atomic model was monitored using PROCHECK (Laskowski et al., 1993). As defined in PROCHECK, 93% of the residues in the model have main-chain torsion angles in the most favored Ramachandran regions. There are no residues in disallowed regions, and three residues in generously allowed regions: Arg-622 in FLGK-A and FLGK-B and Arg-554 in FLGK-A. The overall G-factor score is 0.42.

[0128] The following,table summarizes the X-ray crystallography refinement parameters of the structures of crystalline FLGK and crystalline FLGK:AMP-PCP co-complex of the invention. TABLE 2 Refinement Parameters FLGK: 550 residues, 252 water molecules (4589 atoms) FLGK:AMP-PCP: 550 residues, 238 water molecules, 2 AMP-PCP molecules (4638 atoms) R.m.s.d. d-spacings Reflections R-value^(a) B-values^(b) Model (Å) (N) (%) bonds (Å) angles (°) (Å²) FLGK: 6.0-2.0 42548 21.3 (26.2)^(c) 0.008 1.3 1.6 FLGK:AMP-PCP: 6.0-2.3 26729 20.1 (27.5)^(c) 0.009 1.4 1.7

[0129] Tables 3 and 4, following this page, provide the atomic structure coordinates of unphosphorylated FLGK and unphosphorylated FLGK:AMP-PCP co-complex, respectively. In the Tables, coordinates for both of the FLGK molecules of the dimer comprising the asymmetric unit are provided. The amino acid residue numbers coincide with those used in FIG. 3. In the first FLGK molecule of the dimer the residue number is preceded by a 1, i.e., residue number 464 of the first FLGK molecule of the dimer is denoted by “1464”. TABLE 3 Atomic Structure Coordinates of Unphosphorylated FLGK Atom No. Atom Type A.A. Type A.A. No. X Y Z OCC B ATOM 1 N GLU 1464 −13.639 16.975 8.571 1.00 54.29 ATOM 3 CA GLU 1464 −12.479 17.105 7.695 1.00 52.62 ATOM 4 CB GLU 1464 −11.400 17.974 8.349 1.00 54.64 ATOM 5 C GLU 1464 −11.914 15.738 7.319 1.00 49.74 ATOM 6 O GLU 1464 −11.845 15.407 6.136 1.00 52.04 ATOM 7 N LEU 1465 −11.562 14.925 8.310 1.00 44.95 ATOM 9 CA LEU 1465 −11.018 13.599 8.037 1.00 41.04 ATOM 10 CH LEU 1465 −10.236 13.066 9.235 1.00 40.18 ATOM 11 CG LEU 1465 −8.719 13.196 9.130 1.00 43.70 ATOM 12 CD1 LEU 1465 −8.346 14.654 8.891 1.00 46.74 ATOM 13 CD2 LEU 1465 −8.061 12.671 10.395 1.00 40.72 ATOM 14 C LEU 1465 −12.092 12.594 7.656 1.00 39.18 ATOM 15 O LEU 1465 −13.187 12.590 8.219 1.00 38.05 ATOM 16 N PRO 1466 −11.802 11.748 6.657 1.00 37.20 ATOM 17 CD PRO 1466 −10.597 11.793 5.810 1.00 36.41 ATOM 18 CA PRO 1466 −12.741 10.727 6.189 1.00 36.13 ATOM 19 CB PRO 1466 −12.110 10.262 4.878 1.00 37.50 ATOM 20 CG PRO 1466 −10.629 10.459 5.135 1.00 36.20 ATOM 21 C PRO 1466 −12.846 9.595 7.201 1.00 35.61 ATOM 22 O PRO 1466 −11.847 9.174 7.788 1.00 35.18 ATOM 23 N GLU 1467 −14.060 9.121 7.429 1.00 35.38 ATOM 25 CA GLU 1467 −14.268 8.053 8.377 1.00 35.43 ATOM 26 CB GLU 1467 −15.744 7.965 8.746 1.00 41.10 ATOM 27 CG GLU 1467 −16.375 9.280 9.098 1.00 48.25 ATOM 28 CD GLU 1467 −17.819 9.145 9.596 1.00 50.24 ATOM 29 OE1 GLU 1467 −18.446 8.071 9.378 1.00 52.82 ATOM 30 OE2 GLU 1467 −18.314 10.109 10.230 1.00 51.26 ATOM 31 C GLU 1467 −13.838 6.714 7.801 1.00 32.65 ATOM 32 O GLU 1467 −13.899 6.511 6.591 1.00 35.06 ATOM 33 N ASP 1468 −13.299 5.854 8.659 1.00 30.46 ATOM 35 CA ASP 1468 −12.883 4.516 8.262 1.00 28.85 ATOM 36 CB ASP 1468 −11.384 4.424 7.975 1.00 29.34 ATOM 37 CG ASP 1468 −10.985 3.072 7.408 1.00 27.57 ATOM 38 OD1 ASP 1468 −11.833 2.159 7.359 1.00 27.78 ATOM 39 OD2 ASP 1468 −9.817 2.916 7.003 1.00 30.64 ATOM 40 C ASP 1468 −13.252 3.564 9.384 1.00 29.29 ATOM 41 O ASP 1468 −12.481 3.364 10.336 1.00 27.76 ATOM 42 N PRO 1469 −14.435 2.939 9.268 1.00 28.99 ATOM 43 CD PRO 1469 −15.354 3.091 8.120 1.00 28.09 ATOM 44 CA PRO 1469 −14.971 1.987 10.244 1.00 30.01 ATOM 45 CB PRO 1469 −16.244 1.473 9.553 1.00 33.33 ATOM 46 CG PRO 1469 −16.665 2.630 8.690 1.00 30.53 ATOM 47 C PRO 1469 −14.012 0.848 10.563 1.00 28.96 ATOM 48 O PRO 1469 −14.085 0.251 11.636 1.00 28.52 ATOM 49 N ARG 1470 −13.106 0.556 9.631 1.00 27.59 ATOM 51 CA ARG 1470 −12.139 −0.520 9.810 1.00 27.37 ATOM 52 CB ARG 1470 −11.301 −0.707 8.533 1.00 28.84 ATOM 53 CG ARG 1470 −12.049 −1.279 7.317 1.00 30.57 ATOM 54 CD ARG 1470 −11.137 −1.352 6.068 1.00 26.71 ATOM 55 NE ARG 1470 −10.489 −0.068 5.793 1.00 31.26 ATOM 57 CZ ARG 1470 −9.603 −0.151 4.823 1.00 32.60 ATOM 58 NH1 ARG 1470 −9.241 −0.828 3.999 1.00 33.19 ATOM 61 NH2 ARG 1470 −9.067 1.359 4.686 1.00 28.65 ATOM 64 C ARG 1470 −11.180 −0.285 10.981 1.00 29.21 ATOM 65 0 ARG 1470 −10.757 −1.230 11.641 1.00 28.47 ATOM 66 N TRP 1471 −10.909 0.977 11.280 1.00 27.80 ATOM 68 CA TRP 1471 −9.940 1.314 12.306 1.00 28.62 ATOM 69 CB TRP 1471 −8.729 1.944 11.609 1.00 24.97 ATOM 70 CG TRP 1471 −8.044 0.976 10.728 1.00 24.86 ATOM 71 CD2 TRP 1471 −7.156 −0.060 11.144 1.00 28.00 ATOM 72 CE2 TRP 1471 −6.782 −0.776 9.989 1.00 29.23 ATOM 73 CE3 TRP 1471 −6.642 −0.460 12.389 1.00 26.59 ATOM 74 CD1 TRP 1471 −8.166 0.860 9.374 1.00 27.23 ATOM 75 NE1 TRP 1471 −7.413 −0.192 8.922 1.00 30.10 ATOM 77 CZ2 TRP 1471 −5.912 −1.866 10.036 1.00 28.70 ATOM 78 CZ3 TRP 1471 −5.778 −1.545 12.435 1.00 27.18 ATOM 79 CH2 TRP 1471 −5.424 −2.237 11.266 1.00 27.23 ATOM 80 C TRP 1471 −10.371 2.223 13.440 1.00 28.42 ATOM 81 O TRP 1471 −9.664 2.321 14.442 1.00 26.48 ATOM 82 N GLU 1472 −11.521 2.874 13.293 1.00 28.62 ATOM 84 CA GLU 1472 −11.981 3.823 14.297 1.00 27.16 ATOM 85 CB GLU 1472 −13.245 4.534 13.799 1.00 28.89 ATOM 86 CG GLU 1472 −13.552 5.869 14.520 1.00 29.09 ATOM 87 CD GLU 1472 −12.692 7.042 14.054 1.00 26.43 ATOM 88 OE1 GLU 1472 −12.134 7.009 12.938 1.00 28.59 ATOM 89 OE2 GLU 1472 −12.596 8.024 14.801 1.00 27.28 ATOM 90 C GLU 1472 −12.217 3.269 15.701 1.00 25.10 ATOM 91 O GLU 1472 −12.763 2.196 15.861 1.00 26.48 ATOM 92 N LEU 1473 −11.750 3.991 16.711 1.00 24.65 ATOM 94 CA LEU 1473 −11.962 3.608 18.104 1.00 26.27 ATOM 95 CB LEU 1473 −10.645 3.266 18.817 1.00 28.24 ATOM 96 CG LEU 1473 −10.750 3.025 20.337 1.00 27.23 ATOM 97 CD1 LEU 1473 −11.323 1.636 20.642 1.00 25.23 ATOM 98 CD2 LEU 1473 −9.390 3.183 21.000 1.00 26.33 ATOM 99 C LEU 1473 −12.546 4.856 18.740 1.00 26.52 ATOM 100 O LEU 1473 −12.122 5.973 18.411 1.00 25.16 ATOM 101 N PRO 1474 −13.610 4.703 19.554 1.00 28.52 ATOM 102 CD PRO 1474 −14.435 3.500 19.770 1.00 29.65 ATOM 103 CA PRO 1474 −14.215 5.870 20.207 1.00 29.18 ATOM 104 CB PRO 1474 −15.368 5.251 21.003 1.00 28.58 ATOM 105 CG PRO 1474 −15.768 4.097 20.154 1.00 28.17 ATOM 106 C PRO 1474 −13.173 6.528 21.124 1.00 29.75 ATOM 107 O PRO 1474 −12.427 5.841 21.828 1.00 31.78 ATOM 108 N ARG 1475 −13.107 7.849 21.097 1.00 30.76 ATOM 110 CA ARG 1475 −12.149 8.588 21.900 1.00 32.26 ATOM 111 CE ARG 1475 −12.362 10.083 21.743 1.00 31.58 ATOM 112 CG ARG 1475 −12.178 10.536 20.342 1.00 37.54 ATOM 113 CD ARG 1475 −12.048 12.027 20.206 1.00 36.96 ATOM 114 NE ARG 1475 −11.733 12.317 18.813 1.00 40.07 ATOM 116 CZ ARG 1475 −10.503 12.501 18.352 1.00 37.59 ATOM 117 NH1 ARG 1475 −9.470 12.447 19.186 1.00 34.89 ATOM 120 NH2 ARG 1475 −10.308 12.669 17.049 1.00 34.54 ATOM 123 C ARG 1475 −12.173 8.261 23.371 1.00 35.58 ATOM 124 O ARG 1475 −11.135 8.318 24.036 1.00 37.03 ATOM 125 N ASP 1476 −13.356 7.958 23.889 1.00 36.68 ATOM 127 CA ASP 1476 −13.498 7.647 25.307 1.00 37.07 ATOM 128 CE ASP 1476 −14.967 7.759 25.740 1.00 37.87 ATOM 129 CG ASP 1476 −15.851 6.704 25.115 1.00 38.93 ATOM 130 OD1 ASP 1476 −15.412 6.015 24.179 1.00 43.75 ATOM 131 OD2 ASP 1476 −17.003 6.558 25.563 1.00 45.77 ATOM 132 C ASP 1476 −12.922 6.292 25.701 1.00 35.86 ATOM 133 O ASP 1476 −12.923 5.928 26.878 1.00 37.98 ATOM 134 N ARG 1477 −12.478 5.527 24.711 1.00 33.37 ATOM 136 CA ARG 1477 −11.889 4.221 24.961 1.00 31.84 ATOM 137 CB ARG 1477 −12.214 3.262 23.809 1.00 31.84 ATOM 138 CG ARG 1477 −13.693 2.965 23.580 1.00 29.70 ATOM 139 CD ARG 1477 −14.366 2.365 24.809 1.00 33.88 ATOM 140 NE ARG 1477 −14.596 3.372 25.838 1.00 33.86 ATOM 142 CZ ARG 1477 −14.845 3.102 27.113 1.00 34.14 ATOM 143 NH1 ARG 1477 −14.906 1.846 27.542 1.00 30.58 ATOM 146 NH2 ARG 1477 −15.024 4.102 27.961 1.00 33.14 ATOM 149 C ARG 1477 −10.373 4.338 25.105 1.00 31.30 ATOM 150 O ARG 1477 −9.679 3.362 25.365 1.00 32.32 ATOM 151 N LEU 1478 −9.856 5.544 24.978 1.00 32.85 ATOM 153 CA LEU 1478 −8.426 5.739 25.054 1.00 35.64 ATOM 154 CB LEU 1478 −7.964 6.360 23.737 1.00 34.96 ATOM 155 CG LEU 1478 −6.498 6.291 23.331 1.00 36.36 ATOM 156 CD1 LEU 1478 −6.059 4.833 23.192 1.00 30.71 ATOM 157 CD2 LEU 1478 −6.335 7.048 22.020 1.00 33.97 ATOM 158 C LEU 1478 −8.054 6.625 26.243 1.00 37.60 ATOM 159 O LEU 1478 −8.366 7.815 26.263 1.00 41.20 ATOM 160 N VAL 1479 −7.442 6.023 27.257 1.00 36.52 ATOM 162 CA VAL 1479 −7.008 6.745 28.449 1.00 35.59 ATOM 163 CB VAL 1479 −7.041 5.829 29.688 1.00 35.92 ATOM 164 CG1 VAL 1479 −6.712 6.627 30.926 1.00 39.40 ATOM 165 CG2 VAL 1479 −8.404 5.163 29.825 1.00 34.46 ATOM 166 C VAL 1479 −5.577 7.224 28.197 1.00 35.36 ATOM 167 O VAL 1479 −4.622 6.443 28.269 1.00 32.50 ATOM 168 N LEU 1480 −5.439 8.506 27.878 1.00 37.77 ATOM 170 CA LEU 1480 −4.132 9.086 27.572 1.00 42.77 ATOM 171 CB LEU 1480 −4.298 10.421 26.842 1.00 41.84 ATOM 172 CG LEU 1480 −4.991 10.369 25.471 1.00 42.45 ATOM 173 CD1 LEU 1480 −5.135 11.774 24.924 1.00 42.58 ATOM 174 CD2 LEU 1480 −4.200 9.508 24.502 1.00 43.09 ATOM 175 C LEU 1480 −3.211 9.233 28.778 1.00 45.25 ATOM 176 O LEU 1480 −3.621 9.739 29.822 1.00 45.47 ATOM 177 N GLY 1481 −1.958 8.816 28.612 1.00 46.82 ATOM 179 CA GLY 1481 −1.016 8.889 29.708 1.00 50.47 ATOM 180 C GLY 1481 0.296 9.617 29.472 1.00 52.24 ATOM 181 O GLY 1481 0.360 10.638 28.781 1.00 53.41 ATOM 182 N LYS 1482 1.349 9.070 30.068 1.00 53.64 ATOM 184 CA LYS 1482 2.697 9.627 30.000 1.00 56.19 ATOM 185 CB LYS 1482 3.636 8.776 30.859 1.00 57.19 ATOM 186 CG LYS 1482 5.115 9.023 30.628 1.00 61.02 ATOM 187 CD LYS 1482 5.938 7.831 31.089 1.00 63.12 ATOM 188 CE LYS 1482 5.494 6.547 30.395 1.00 61.98 ATOM 189 NZ LYS 1482 6.252 5.368 30.899 1.00 63.38 ATOM 193 C LYS 1482 3.297 9.795 28.604 1.00 56.56 ATOM 194 O LYS 1482 3.291 8.868 27.791 1.00 55.03 ATOM 195 N PRO 1483 3.852 10.983 28.323 1.00 58.31 ATOM 196 CD PRO 1483 3.859 12.191 29.167 1.00 56.98 ATOM 197 CA PRO 1483 4.465 11.254 27.020 1.00 59.52 ATOM 198 CB PRO 1483 4.910 12.711 27.155 1.00 58.75 ATOM 199 CG PRO 1483 3.927 13.278 28.141 1.00 58.79 ATOM 200 C PRO 1483 5.673 10.335 26.834 1.00 61.17 ATOM 201 O PRO 1483 6.509 10.216 27.731 1.00 61.31 ATOM 202 N LEU 1484 5.728 9.643 25.702 1.00 64.31 ATOM 204 CA LEU 1484 6.838 8.738 25.408 1.00 67.77 ATOM 205 CB LEU 1484 6.349 7.512 24.640 1.00 67.66 ATOM 206 CG LEU 1484 5.415 6.558 25.386 1.00 69.00 ATOM 207 CD1 LEU 1484 4.943 5.457 24.445 1.00 66.76 ATOM 208 CD2 LEU 1484 6.126 5.972 26.604 1.00 67.77 ATOM 209 C LEU 1484 7.934 9.431 24.608 1.00 70.82 ATOM 210 O LEU 1484 9.117 9.115 24.759 1.00 71.82 ATOM 211 N GLY 1485 7.534 10.357 23.742 1.00 73.28 ATOM 213 CA GLY 1485 8.492 11.077 22.922 1.00 74.53 ATOM 214 C GLY 1485 7.819 11.754 21.747 1.00 75.19 ATOM 215 O GLY 1485 6.635 12.090 21.822 1.00 75.61 ATOM 216 N GLN 1491 4.406 14.274 18.638 1.00 50.72 ATOM 218 CA GLN 1491 4.042 13.876 19.994 1.00 47.33 ATOM 219 CB GLN 1491 3.033 14.869 20.587 1.00 46.67 ATOM 220 C GLN 1491 3.486 12.449 20.073 1.00 46.66 ATOM 221 O GLN 1491 2.581 12.074 19.323 1.00 45.20 ATOM 222 N VAL 1492 4.072 11.650 20.960 1.00 45.41 ATOM 224 CA VAL 1492 3.646 10.274 21.184 1.00 43.83 ATOM 225 CB VAL 1492 4.680 9.244 20.709 1.00 41.60 ATOM 226 CG1 VAL 1492 4.138 7.849 20.937 1.00 41.35 ATOM 227 CG2 VAL 1492 5.007 9.445 19.237 1.00 42.72 ATOM 228 C VAL 1492 3.458 10.084 22.683 1.00 44.45 ATOM 229 O VAL 1492 4.335 10.437 23.482 1.00 43.86 ATOM 230 N VAL 1493 2.309 9.548 23.070 1.00 42.67 ATOM 232 CA VAL 1493 2.029 9.321 24.477 1.00 41.05 ATOM 233 CB VAL 1493 0.884 10.242 25.013 1.00 40.64 ATOM 234 CG1 VAL 1493 −1.177 11.693 24.722 1.00 42.40 ATOM 235 CG2 VAL 1493 0.459 9.844 24.427 1.00 43.36 ATOM 236 C VAL 1493 1.626 7.880 24.704 1.00 40.09 ATOM 237 O VAL 1493 1.129 7.212 23.796 1.00 39.99 ATOM 238 N LEU 1494 1.927 7.374 25.890 1.00 37.10 ATOM 240 CA LEU 1494 1.535 6.036 26.250 1.00 35.08 ATOM 241 CB LEU 1494 2.359 5.542 27.440 1.00 35.57 ATOM 242 CG LEU 1494 2.036 4.161 28.007 1.00 36.87 ATOM 243 CD1 LEU 1494 2.123 3.085 26.931 1.00 36.90 ATOM 244 CD2 LEU 1494 2.998 3.860 29.143 1.00 41.99 ATOM 245 C LEU 1494 0.077 6.236 26.648 1.00 33.31 ATOM 246 O LEU 1494 −0.311 7.318 27.097 1.00 32.93 ATOM 247 N ALA 1495 −0.740 5.219 26.435 1.00 33.35 ATOM 249 CA ALA 1495 −2.147 5.292 26.773 1.00 30.67 ATOM 250 CB ALA 1495 −2.923 5.937 25.637 1.00 30.35 ATOM 251 C ALA 1495 −2.661 3.893 27.025 1.00 29.97 ATOM 252 O ALA 1495 −1.944 2.909 26.840 1.00 28.15 ATOM 253 N GLU 1496 −3.898 3.813 27.488 1.00 30.37 ATOM 255 CA GLU 1496 −4.537 2.536 27.745 1.00 31.47 ATOM 256 CB GLU 1496 −4.862 2.392 29.223 1.00 32.48 ATOM 257 CG GLU 1496 −3.627 2.239 30.093 1.00 37.81 ATOM 258 CD GLU 1496 −3.938 2.426 31.565 1.00 41.09 ATOM 259 OE1 GLU 1496 −4.328 3.548 31.944 1.00 41.53 ATOM 260 OE2 GLU 1496 −3.797 1.453 32.341 1.00 44.12 ATOM 261 C GLU 1496 −5.806 2.524 26.916 1.00 32.72 ATOM 262 O GLU 1496 −6.586 3.478 26.954 1.00 33.91 ATOM 263 N ALA 1497 −5.953 1.494 26.094 1.00 31.06 ATOM 265 CA ALA 1497 −7.117 1.353 25.239 1.00 32.33 ATOM 266 CB ALA 1497 −6.691 0.879 23.859 1.00 29.56 ATOM 267 C ALA 1497 −8.056 0.343 25.885 1.00 32.26 ATOM 268 O ALA 1497 −7.648 −0.773 26.197 1.00 33.55 ATOM 269 N ILE 1498 −9.286 0.759 26.160 1.00 32.99 ATOM 271 CA ILE 1498 −10.276 −0.126 26.766 1.00 34.00 ATOM 272 CB ILE 1498 −11.329 0.668 27.592 1.00 34.69 ATOM 273 CG2 ILE 1498 −12.341 −0.288 28.240 1.00 34.24 ATOM 274 CG1 ILE 1498 −10.647 1.496 28.686 1.00 33.56 ATOM 275 CD1 ILE 1498 −11.543 2.572 29.258 1.00 31.25 ATOM 276 C ILE 1498 −10.994 −0.830 25.624 1.00 35.71 ATOM 277 O ILE 1498 −11.618 −0.181 24.786 1.00 34.88 ATOM 278 N GLY 1499 −10.890 −2.147 25.573 1.00 40.43 ATOM 280 CA GLY 1499 −11.553 −2.884 24.516 1.00 47.63 ATOM 281 C GLY 1499 −10.670 −3.233 23.330 1.00 53.08 ATOM 282 O GLY 1499 −9.934 −4.226 23.380 1.00 54.97 ATOM 283 N LEU 1500 −10.713 −2.394 22.294 1.00 54.18 ATOM 285 CA LEU 1500 −9.957 −2.603 21.055 1.00 55.26 ATOM 286 CB LEU 1500 −8.444 −2.726 21.305 1.00 55.39 ATOM 287 CG LEU 1500 −7.562 −1.472 21.241 1.00 54.27 ATOM 288 CD1 LEU 1500 −6.110 −1.891 21.367 1.00 52.89 ATOM 289 CD2 LEU 1500 −7.768 −0.711 19.935 1.00 50.91 ATOM 290 C LEU 1500 −10.453 −3.830 20.288 1.00 55.39 ATOM 291 O LEU 1500 −10.376 −4.963 20.774 1.00 56.23 ATOM 292 N PRO 1505 −13.315 −5.836 25.394 1.00 53.03 ATOM 293 CD PRO 1505 −13.945 −7.148 25.167 1.00 55.12 ATOM 294 CA PRO 1505 −14.306 −4.848 25.846 1.00 50.62 ATOM 295 CB PRO 1505 −15.635 −5.607 25.715 1.00 50.09 ATOM 296 CG PRO 1505 −15.241 −7.031 25.950 1.00 52.18 ATOM 297 C PRO 1505 −14.039 −4.348 27.273 1.00 46.35 ATOM 298 O PRO 1505 −14.065 −3.143 27.524 1.00 45.82 ATOM 299 N ASN 1506 −13.711 −5.261 28.181 1.00 42.76 ATOM 301 CA ASN 1506 −13.433 −4.892 29.566 1.00 45.29 ATOM 302 CB ASN 1506 −14.283 −5.728 30.529 1.00 45.92 ATOM 303 CG ASN 1506 −15.752 −5.395 30.441 1.00 46.17 ATOM 304 OD1 ASN 1506 −16.132 −4.232 30.390 1.00 48.57 ATOM 305 ND2 ASN 1506 −16.589 −6.418 30.406 1.00 48.63 ATOM 308 C ASN 1506 −11.954 −5.008 29.939 1.00 45.33 ATOM 309 O ASN 1506 −11.597 −5.084 31.121 1.00 44.53 ATOM 310 N ARG 1507 −11.100 −5.010 28.924 1.00 45.63 ATOM 312 CA ARG 1507 −9.660 −5.122 29.117 1.00 45.57 ATOM 313 CB ARG 1507 −9.131 −6.354 28.375 1.00 53.33 ATOM 314 CG ARG 1507 −9.407 −7.685 29.043 1.00 61.39 ATOM 315 CD ARG 1507 −8.336 −8.028 30.063 1.00 67.74 ATOM 316 NE ARG 1507 −8.525 −9.376 30.585 1.00 74.64 ATOM 318 CZ ARG 1507 −7.970 −9.842 31.701 1.00 80.01 ATOM 319 NH1 ARG 1507 −7.166 −9.075 32.433 1.00 80.04 ATOM 322 NH2 ARG 1507 −8.268 −11.068 32.115 1.00 83.41 ATOM 325 C ARG 1507 −8.964 −3.897 28.555 1.00 40.94 ATOM 326 O ARG 1507 −9.370 −3.375 27.517 1.00 37.60 ATOM 327 N VAL 1508 −7.956 −3.409 29.267 1.00 39.33 ATOM 329 CA VAL 1508 −7.190 −2.269 28.789 1.00 37.26 ATOM 330 CB VAL 1508 −6.854 −1.224 29.905 1.00 36.25 ATOM 331 CG1 VAL 1508 −8.124 −0.739 30.571 1.00 39.63 ATOM 332 CG2 VAL 1508 −5.903 −1.796 30.928 1.00 36.92 ATOM 333 C VAL 1508 −5.898 −2.818 28.188 1.00 34.38 ATOM 334 O VAL 1508 −5.387 −3.851 28.630 1.00 32.85 ATOM 335 N THR 1509 −5.406 −2.140 27.159 1.00 30.47 ATOM 337 CA THR 1509 −4.174 −2.523 26.491 1.00 31.65 ATOM 338 CB THR 1509 −4.455 −2.959 25.027 1.00 34.13 ATOM 339 OG1 THR 1509 −5.426 −4.013 25.018 1.00 40.74 ATOM 341 CG2 THR 1509 −3.184 −3.458 24.345 1.00 31.06 ATOM 342 C THR 1509 −3.270 −1.299 26.461 1.00 28.38 ATOM 343 O THR 1509 −3.716 −0.219 26.104 1.00 27.78 ATOM 344 N LYS 1510 −2.023 −1.442 26.896 1.00 29.48 ATOM 346 CA LYS 1510 −1.101 −0.312 26.835 1.00 30.54 ATOM 347 CB LYS 1510 0.172 −0.558 27.635 1.00 27.88 ATOM 348 CG LYS 1510 −0.037 −0.600 29.118 1.00 33.91 ATOM 349 CD LYS 1510 1.284 −0.759 29.840 1.00 40.30 ATOM 350 CE LYS 1510 1.145 −1.674 31.062 1.00 46.24 ATOM 351 NZ LYS 1510 0.338 −1.096 32.187 1.00 49.09 ATOM 355 C LYS 1510 −0.757 −0.166 25.365 1.00 28.64 ATOM 356 O LYS 1510 −0.402 −1.142 24.704 1.00 28.76 ATOM 357 N VAL 1511 −0.902 1.048 24.856 1.00 29.34 ATOM 359 CA VAL 1511 −0.627 1.347 23.463 1.00 29.79 ATOM 360 CB VAL 1511 −1.951 1.457 22.658 1.00 27.14 ATOM 361 CG1 VAL 1511 −2.681 0.111 22.657 1.00 24.56 ATOM 362 CG2 VAL 1511 −2.837 2.561 23.243 1.00 22.15 ATOM 363 C VAL 1511 0.123 2.672 23.361 1.00 29.83 ATOM 364 O VAL 1511 0.213 3.413 24.338 1.00 33.14 ATOM 365 N ALA 1512 0.705 2.939 22.196 1.00 27.86 ATOM 367 CA ALA 1512 1.405 4.192 21.962 1.00 25.55 ATOM 368 CB ALA 1512 2.743 3.935 21.297 1.00 24.69 ATOM 369 C ALA 1512 0.500 5.009 21.057 1.00 25.25 ATOM 370 O ALA 1512 −0.061 4.483 20.107 1.00 27.18 ATOM 371 N VAL 1513 0.340 6.289 21.360 1.00 29.63 ATOM 373 CA VAL 1513 −0.520 7.165 20.573 1.00 32.66 ATOM 374 CB VAL 1513 −1.704 7.713 21.422 1.00 32.47 ATOM 375 CG1 VAL 1513 −2.609 8.585 20.574 1.00 32.29 ATOM 376 CG2 VAL 1513 −2.508 6.559 22.031 1.00 32.15 ATOM 377 C VAL 1513 0.238 8.334 19.938 1.00 34.67 ATOM 378 O VAL 1513 0.792 9.185 20.635 1.00 34.65 ATOM 379 N LYS 1514 0.207 8.367 18.605 1.00 36.88 ATOM 381 CA LYS 1514 0.859 9.390 17.789 1.00 36.43 ATOM 382 CB LYS 1514 1.349 8.764 16.489 1.00 36.37 ATOM 383 CG LYS 1514 2.250 7.563 16.697 1.00 39.49 ATOM 384 CD LYS 1514 2.559 6.854 15.390 1.00 45.29 ATOM 385 CE LYS 1514 3.080 7.815 14.331 1.00 50.70 ATOM 386 NZ LYS 1514 4.212 8.685 14.798 1.00 51.41 ATOM 390 C LYS 1514 −0.121 10.496 17.459 1.00 36.75 ATOM 391 O LYS 1514 −1.228 10.234 16.978 1.00 35.42 ATOM 392 N MET 1515 0.294 11.731 17.700 1.00 38.12 ATOM 394 CA MET 1515 −0.545 12.882 17.432 1.00 41.90 ATOM 395 CB MET 1515 −1.371 13.238 18.668 1.00 43.08 ATOM 396 CG MET 1515 −0.536 13.601 19.880 1.00 45.01 ATOM 397 SD MET 1515 −1.561 13.784 21.324 1.00 46.03 ATOM 398 CE MET 1515 −1.675 12.072 21.885 1.00 44.02 ATOM 399 C MET 1515 0.314 14.065 17.021 1.00 44.65 ATOM 400 O MET 1515 1.543 14.013 17.094 1.00 45.64 ATOM 401 N LEU 1516 −0.347 15.123 16.568 1.00 47.08 ATOM 403 CA LEU 1516 0.329 16.337 16.134 1.00 48.08 ATOM 404 CB LEU 1516 −0.500 17.033 15.054 1.00 45.50 ATOM 405 CG LEU 1516 −0.764 16.265 13.764 1.00 43.22 ATOM 406 CD1 LEU 1516 −1.783 17.014 12.946 1.00 40.32 ATOM 407 CD2 LEU 1516 0.540 16.072 12.991 1.00 43.78 ATOM 408 C LEU 1516 0.516 17.302 17.297 1.00 51.27 ATOM 409 O LEU 1516 0.214 17.249 18.291 1.00 50.37 ATOM 410 N LYS 1517 1.491 18.191 17.157 1.00 55.47 ATOM 412 CA LYS 1517 1.757 19.207 18.168 1.00 59.10 ATOM 413 CB LYS 1517 3.203 19.702 18.068 1.00 61.61 ATOM 414 CG LYS 1517 4.251 18.669 18.462 1.00 64.82 ATOM 415 CD LYS 1517 5.635 19.109 18.018 1.00 67.42 ATOM 416 CE LYS 1517 6.696 18.102 18.432 1.00 71.76 ATOM 417 NZ LYS 1517 8.021 18.411 17.812 1.00 73.57 ATOM 421 C LYS 1517 0.794 20.365 17.920 1.00 59.91 ATOM 422 O LYS 1517 0.187 20.456 16.852 1.00 59.88 ATOM 423 N SER 1518 0.686 21.267 18.886 1.00 61.85 ATOM 425 CA SER 1518 −0.216 22.409 18.760 1.00 63.70 ATOM 426 CB SER 1518 −0.158 23.274 20.024 1.00 64.21 ATOM 427 C SER 1518 0.0792 3.263 17.529 1.00 64.37 ATOM 428 O SER 1518 −0.841 23.757 16.875 1.00 66.16 ATOM 429 N ASP 1519 1.359 23.410 17.202 1.00 64.15 ATOM 431 CA ASP 1519 1.767 24.217 16.054 1.00 64.55 ATOM 432 CB ASP 1519 3.109 24.897 16.343 1.00 65.84 ATOM 433 C ASP 1519 1.858 23.441 24.742 1.00 63.95 ATOM 434 O ASP 1519 2.432 23.931 13.769 1.00 64.95 ATOM 435 N ALA 1520 1.303 22.232 14.719 1.00 62.57 ATOM 437 CA ALA 1520 1.329 21.398 13.521 1.00 60.34 ATOM 438 CB ALA 1520 0.704 20.039 13.810 1.00 60.53 ATOM 439 C ALA 1520 0.616 22.062 12.353 1.00 58.21 ATOM 440 O ALA 1520 −0.464 22.631 12.506 1.00 58.32 ATOM 441 N THR 1521 1.241 22.001 11.186 1.00 55.96 ATOM 443 CA THR 1521 0.673 22.582 9.981 1.00 54.98 ATOM 444 CB THR 1521 1.783 23.013 9.031 1.00 53.84 ATOM 445 OG1 THR 1521 2.554 21.862 8.659 1.00 55.84 ATOM 447 CG2 THR 1521 2.693 24.026 9.703 1.00 55.01 ATOM 448 C THR 1521 −0.184 21.545 9.261 1.00 54.25 ATOM 449 O THR 1521 −0.190 20.371 9.629 1.00 54.74 ATOM 450 N GLU 1522 −0.877 21.974 8.212 1.00 53.32 ATOM 452 CA GLU 1522 −1.702 21.066 7.423 1.00 52.64 ATOM 453 CB GLU 1522 −2.472 21.829 6.339 1.00 53.55 ATOM 454 C GLU 1522 −0.793 20.012 6.780 1.00 51.95 ATOM 455 O GLU 1522 −1.226 18.895 6.504 1.00 53.28 ATOM 456 N LYS 1523 0.464 20.377 6.544 1.00 48.66 ATOM 458 CA LYS 1523 1.429 19.460 5.963 1.00 46.30 ATOM 459 CB LYS 1523 2.730 20.201 5.620 1.00 48.30 ATOM 460 CG LYS 1523 3.889 19.308 5.164 1.00 49.58 ATOM 461 CD LYS 1523 3.487 18.388 4.016 1.00 50.87 ATOM 462 CE LYS 1523 4.688 17.635 3.466 1.00 54.08 ATOM 463 NZ LYS 1523 4.271 16.629 2.440 1.00 57.87 ATOM 467 C LYS 1523 1.699 18.391 7.006 1.00 43.89 ATOM 468 O LYS 1523 1.747 17.202 6.697 1.00 43.92 ATOM 469 N ASP 1524 1.857 18.828 8.249 1.00 42.71 ATOM 471 CA ASP 1524 2.114 17.915 9.351 1.00 42.11 ATOM 472 CB ASP 1524 2.313 18.701 10.653 1.00 44.94 ATOM 473 CG ASP 1524 3.623 19.490 10.673 1.00 48.90 ATOM 474 OD1 ASP 1524 3.692 20.512 11.392 1.00 51.88 ATOM 475 OD2 ASP 1524 4.590 19.084 9.990 1.00 50.06 ATOM 476 C ASP 1524 0.956 16.931 9.481 1.00 39.85 ATOM 477 O ASP 1524 1.164 15.738 9.748 1.00 39.01 ATOM 478 N LEU 1525 −0.261 17.438 9.296 1.00 38.32 ATOM 480 CA LEU 1525 −1.461 16.610 9.355 1.00 36.16 ATOM 481 CB LEU 1525 −2.720 17.470 9.200 1.00 35.13 ATOM 482 CG LEU 1525 −4.081 16.760 9.186 1.00 34.70 ATOM 483 CD1 LEU 1525 −4.184 15.668 10.252 1.00 36.15 ATOM 484 CD2 LEU 1525 −5.162 17.789 9.395 1.00 32.96 ATOM 485 C LEW 1525 −1.406 15.560 8.254 1.00 34.31 ATOM 486 O LEU 1525 −1.575 14.377 8.518 1.00 33.34 ATOM 487 N SER 1526 −1.136 16.005 7.030 1.00 36.40 ATOM 489 CA SER 1526 −1.039 15.128 5.865 1.00 37.16 ATOM 490 CB SER 1526 −0.669 15.931 4.618 1.00 38.84 ATOM 491 OG SER 1526 −1.736 16.779 4.245 1.00 49.61 ATOM 493 C SER 1526 −0.021 14.016 6.044 1.00 35.90 ATOM 494 O SER 1526 −0.273 12.873 5.670 1.00 36.68 ATOM 495 N ASP 1527 1.142 14.349 6.591 1.00 35.89 ATOM 497 CA ASP 1527 2.177 13.342 6.796 1.00 35.25 ATOM 498 CB ASP 1527 3.497 13.998 7.201 1.00 35.58 ATOM 499 CG ASP 1527 4.100 14.850 6.081 1.00 37.19 ATOM 500 OD1 ASP 1527 3.750 14.653 4.895 1.00 37.38 ATOM 501 OD2 ASP 1527 4.932 15.726 6.395 1.00 42.93 ATOM 502 C ASP 1527 1.749 12.274 7.799 1.00 31.77 ATOM 503 O ASP 1527 2.000 11.090 7.594 1.00 30.58 ATOM 504 N LEU 1528 1.055 12.684 8.853 1.00 31.80 ATOM 506 CA LEU 1528 0.581 11.730 9.857 1.00 33.53 ATOM 507 CB LEU 1528 −0.002 12.471 11.076 1.00 32.20 ATOM 508 CG LEU 1528 −0.440 11.623 12.275 1.00 32.63 ATOM 509 CD1 LEU 1528 0.705 10.708 12.709 1.00 33.09 ATOM 510 CD2 LEU 1528 −0.891 12.512 13.426 1.00 31.52 ATOM 511 C LEU 1528 −0.468 10.792 9.235 1.00 32.89 ATOM 512 O LEU 1528 −0.494 9.589 9.521 1.00 32.39 ATOM 513 N ILE 1529 −1.336 11.357 8.393 1.00 33.72 ATOM 515 CA ILE 1529 −2.376 10.591 7.711 1.00 30.48 ATOM 516 CB ILE 1529 −3.336 11.505 6.895 1.00 28.85 ATOM 517 CG2 ILE 1529 −4.229 10.662 5.997 1.00 28.54 ATOM 518 CG1 ILE 1529 −4.200 12.344 7.843 1.00 29.52 ATOM 519 CD1 ILE 1529 −5.143 13.308 7.133 1.00 32.07 ATOM 520 C ILE 1529 −1.698 9.608 6.768 1.00 31.50 ATOM 521 O ILE 1529 −2.009 8.419 6.780 1.00 30.75 ATOM 522 N SER 1530 −0.749 10.100 5.974 1.00 33.28 ATOM 524 CA SER 1530 −0.011 9.250 5.038 1.00 32.48 ATOM 525 CB SER 1530 1.114 10.042 4.368 1.00 37.20 ATOM 526 OG SER 1530 0.604 11.218 3.766 1.00 49.93 ATOM 528 C SER 1530 0.583 8.045 5.756 1.00 29.05 ATOM 529 O SER 1530 0.397 6.909 5.316 1.00 28.66 ATOM 530 N GLU 1531 1.259 8.290 6.878 1.00 28.21 ATOM 532 CA GLU 1531 1.880 7.207 7.631 1.00 27.30 ATOM 533 CB GLU 1531 2.656 7.733 8.839 1.00 28.90 ATOM 534 CG GLU 1531 3.271 6.609 9.672 1.00 27.17 ATOM 535 CD GLU 1531 4.047 7.081 10.886 1.00 30.07 ATOM 536 OE1 GLU 1531 4.779 6.244 11.448 1.00 34.78 ATOM 537 OE2 GLU 1531 3.931 8.256 11.291 1.00 31.96 ATOM 538 C GLU 1531 0.870 6.162 8.072 1.00 27.73 ATOM 539 O GLU 1531 1.160 4.961 8.028 1.00 28.72 ATOM 540 N MET 1532 −0.286 6.621 8.555 1.00 29.78 ATOM 542 CA MET 1532 −1.373 5.734 8.990 1.00 28.79 ATOM 543 CB MET 1532 −2.501 6.553 9.646 1.00 28.90 ATOM 544 CG MET 1532 −3.763 5.741 9.993 1.00 29.73 ATOM 545 SD MET 1532 −5.089 6.693 10.765 1.00 30.19 ATOM 546 CE MET 1532 −5.455 7.870 9.494 1.00 26.70 ATOM 547 C MET 1532 −1.935 4.937 7.796 1.00 28.34 ATOM 548 O MET 1532 −2.166 3.730 7.893 1.00 26.62 ATOM 549 N GLU 1533 −2.165 5.624 6.678 1.00 28.85 ATOM 551 CA GLU 1533 −2.684 4.984 5.467 1.00 28.24 ATOM 552 CB GLU 1533 −2.936 6.027 4.384 1.00 25.42 ATOM 553 CG GLU 1533 −4.099 6.956 4.719 1.00 30.05 ATOM 554 CD GLU 1533 −5.393 6.201 5.021 1.00 29.47 ATOM 555 OE1 GLU 1533 −5.794 5.336 4.211 1.00 29.01 ATOM 556 OE2 GLU 1533 −6.011 6.472 6.073 1.00 33.98 ATOM 557 C GLU 1533 −1.694 3.944 4.968 1.00 28.01 ATOM 558 O GLU 1533 −2.072 2.845 4.573 1.00 27.39 ATOM 559 N MET 1534 −0.416 4.293 5.036 1.00 29.06 ATOM 561 CA MET 1534 0.662 3.413 4.621 1.00 29.74 ATOM 562 CB MET 1534 1.992 4.155 4.755 1.00 33.16 ATOM 563 CG MET 1534 3.198 3.270 4.682 1.00 42.88 ATOM 564 SD MET 1534 3.805 3.127 3.042 1.00 50.20 ATOM 565 CE MET 1534 5.137 4.169 3.159 1.00 42.64 ATOM 566 C MET 1534 0.641 2.156 5.493 1.00 26.90 ATOM 567 O MET 1534 0.755 1.038 4.990 1.00 27.05 ATOM 568 N MET 1535 0.512 2.348 6.803 1.00 25.42 ATOM 570 CA MET 1535 0.437 1.233 7.737 1.00 25.88 ATOM 571 CB MET 1535 0.325 1.741 9.181 1.00 27.63 ATOM 572 CG MET 1535 1.607 2.391 9.737 1.00 27.26 ATOM 573 SD MET 1535 1.584 2.561 11.564 1.00 29.49 ATOM 574 CE MET 1535 1.294 4.255 11.699 1.00 28.22 ATOM 575 C MET 1535 −0.754 0.324 7.396 1.00 26.28 ATOM 576 O MET 1535 −0.645 −0.908 7.469 1.00 25.93 ATOM 577 N LYS 1536 −1.890 0.928 7.032 1.00 27.19 ATOM 579 CA LYS 1536 −3.087 0.162 6.647 1.00 27.20 ATOM 580 CB LYS 1536 −4.257 1.088 6.310 1.00 25.29 ATOM 581 CG LYS 1536 −4.897 1.770 7.491 1.00 23.86 ATOM 582 CD LYS 1536 −5.884 2.820 7.017 1.00 22.16 ATOM 583 CE LYS 1536 −6.460 3.588 8.174 1.00 22.25 ATOM 584 NZ LYS 1536 −7.484 4.541 7.713 1.00 23.40 ATOM 588 C LYS 1536 −2.785 −0.699 5.423 1.00 24.52 ATOM 589 O LYS 1536 −3.069 −1.889 5.403 1.00 26.61 ATOM 590 N MET 1537 −2.183 −0.093 4.411 1.00 27.12 ATOM 592 CA MET 1537 −1.843 −0.815 3.194 1.00 28.06 ATOM 593 CB MET 1537 −1.269 0.147 2.147 1.00 30.36 ATOM 594 CG MET 1537 −2.265 1.164 1.591 1.00 36.31 ATOM 595 SD MET 1537 −3.699 0.444 0.727 1.00 42.19 ATOM 596 CE MET 1537 −2.912 −0.057 −0.793 1.00 36.22 ATOM 597 C MET 1537 −0.857 −1.952 3.447 1.00 26.98 ATOM 598 O MET 1537 −1.060 −3.065 2.963 1.00 25.34 ATOM 599 N ILE 1538 0.188 −1.678 4.229 1.00 27.69 ATOM 601 CA ILE 1538 1.234 −2.674 4.535 1.00 25.39 ATOM 602 CB ILE 1538 2.454 −2.006 5.255 1.00 24.42 ATOM 603 CG2 ILE 1538 3.424 −3.051 5.811 1.00 25.28 ATOM 604 CG1 ILE 1538 3.223 −1.131 4.269 1.00 23.88 ATOM 605 CD1 ILE 1538 4.373 −0.372 4.901 1.00 27.19 ATOM 606 C ILE 1538 0.760 −3.922 5.292 1.00 25.59 ATOM 607 O ILE 1538 1.242 −5.033 5.035 1.00 26.11 ATOM 608 N GLY 1539 −0.193 −3.767 6.208 1.00 26.13 ATOM 610 CA GLY 1539 −0.661 −4.940 6.934 1.00 25.25 ATOM 611 C GLY 1539 0.191 −5.280 8.149 1.00 26.77 ATOM 612 O GLY 1539 1.214 −4.637 8.414 1.00 25.42 ATOM 613 N LYS 1540 −0.204 −6.327 8.862 1.00 25.62 ATOM 615 CA LYS 1540 0.467 −6.716 10.092 1.00 26.38 ATOM 616 CB LYS 1540 −0.552 −7.283 11.084 1.00 27.15 ATOM 617 CG LYS 1540 −1.573 −6.303 11.550 1.00 34.23 ATOM 618 CD LYS 1540 −2.528 −6.943 12.546 1.00 40.69 ATOM 619 CE LYS 1540 −3.559 −5.927 13.057 1.00 44.08 ATOM 620 NZ LYS 1540 −2.956 −4.800 13.833 1.00 44.05 ATOM 624 C LYS 1540 1.609 −7.705 10.014 1.00 24.37 ATOM 625 O LYS 1540 1.627 −8.600 9.181 1.00 26.12 ATOM 626 N HIS 1541 2.545 −7.538 10.936 1.00 24.41 ATOM 628 CA HIS 1541 3.666 −8.440 11.091 1.00 25.41 ATOM 629 CB HIS 1541 4.772 −8.228 10.057 1.00 21.88 ATOM 630 CG HIS 1541 5.798 −9.320 10.068 1.00 22.68 ATOM 631 CD2 HIS 1541 5.823 −10.522 9.444 1.00 21.40 ATOM 632 ND1 HIS 1541 6.939 −9.268 10.843 1.00 22.12 ATOM 634 CE1 HIS 1541 7.619 −10.389 10.697 1.00 24.78 ATOM 635 NE2 HIS 1541 6.966 −11.167 9.854 1.00 27.00 ATOM 637 C HIS 1541 4.234 −8.328 12.494 1.00 25.47 ATOM 638 O HIS 1541 4.364 −7.239 13.050 1.00 26.77 ATOM 639 N LYS 1542 4.560 −9.476 13.063 1.00 26.38 ATOM 641 CA LYS 1542 5.127 −9.552 14.401 1.00 30.07 ATOM 642 CB LYS 1542 5.515 −11.003 14.692 1.00 31.38 ATOM 643 CG LYS 1542 6.061 −11.252 16.077 1.00 42.79 ATOM 644 CD LYS 1542 6.289 −12.735 16.294 1.00 50.84 ATOM 645 CE LYS 1542 7.041 −13.374 15.114 1.00 56.75 ATOM 646 NZ LYS 1542 7.511 −14.763 15.424 1.00 61.29 ATOM 650 C LYS 1542 6.342 −8.652 14.624 1.00 27.65 ATOM 651 O LYS 1542 6.519 −8.113 15.711 1.00 26.83 ATOM 652 N ASN 1543 7.146 −8.445 13.585 1.00 27.20 ATOM 654 CA ASN 1543 8.354 −7.642 13.735 1.00 25.50 ATOM 655 CB ASN 1543 9.578 −8.431 13.260 1.00 25.59 ATOM 656 CG ASN 1543 9.712 −9.767 13.974 1.00 22.64 ATOM 657 OD1 ASN 1543 9.522 −10.821 13.371 1.00 26.76 ATOM 658 ND2 ASN 1543 9.970 −9.727 15.273 1.00 25.56 ATOM 661 C ASN 1543 8.374 −6.213 13.226 1.00 25.48 ATOM 662 O ASN 1543 9.417 −5.692 12.842 1.00 24.58 ATOM 663 N ILE 1544 7.209 −5.575 13.244 1.00 24.60 ATOM 665 CA ILE 1544 7.065 −4.177 12.868 1.00 22.32 ATOM 666 CB ILE 1544 6.524 −3.972 11.409 1.00 25.82 ATOM 667 CG2 ILE 1544 7.401 −4.720 10.403 1.00 24.24 ATOM 668 CG1 ILE 1544 5.057 −4.411 11.279 1.00 26.04 ATOM 669 CD1 ILE 1544 4.446 −4.121 9.901 1.00 23.20 ATOM 670 C ILE 1544 6.075 −3.598 13.881 1.00 22.37 ATOM 671 O ILE 1544 5.364 −4.345 14.559 1.00 21.68 ATOM 672 N ILE 1545 6.111 −2.290 14.076 1.00 23.72 ATOM 674 CA ILE 1545 5.169 −1.650 14.989 1.00 25.92 ATOM 675 CB ILE 1545 5.602 −0.199 15.364 1.00 27.24 ATOM 676 CG2 ILE 1545 4.452 0.554 16.035 1.00 22.76 ATOM 677 CG1 ILE 1545 6.839 −0.219 16.285 1.00 25.57 ATOM 678 CD1 ILE 1545 6.591 −0.797 17.686 1.00 24.66 ATOM 679 C ILE 1545 3.877 −1.612 14.179 1.00 26.03 ATOM 680 O ILE 1545 3.823 −0.988 13.122 1.00 25.70 ATOM 681 N ASN 1546 2.849 −2.293 14.669 1.00 24.79 ATOM 683 CA ASN 1546 1.577 −2.354 13.956 1.00 25.51 ATOM 684 CB ASN 1546 0.922 −3.727 14.137 1.00 25.17 ATOM 685 CG ASN 1546 1.730 −4.839 13.539 1.00 21.67 ATOM 686 OD1 ASN 1546 1.856 −4.947 12.329 1.00 24.29 ATOM 687 ND2 ASN 1546 2.278 −5.686 14.384 1.00 22.24 ATOM 690 C ASN 1546 0.578 −1.276 14.349 1.00 26.85 ATOM 691 O ASN 1546 0.630 −0.724 15.453 1.00 28.67 ATOM 692 N LEU 1547 −0.301 −0.956 13.407 1.00 27.70 ATOM 694 CA LEU 1547 −1.357 0.019 13.622 1.00 27.64 ATOM 695 CB LEU 1547 −1.945 0.481 12.284 1.00 24.87 ATOM 696 CG LEU 1547 −3.173 1.400 12.337 1.00 23.25 ATOM 697 CD1 LEU 1547 −2.790 2.763 12.929 1.00 23.76 ATOM 698 CD2 LEU 1547 −3.757 1.569 10.923 1.00 23.47 ATOM 699 C LEU 1547 −2.415 −0.771 14.396 1.00 27.27 ATOM 700 O LEU 1547 −2.663 −1.952 14.103 1.00 25.27 ATOM 701 N LEU 1548 −3.000 −0.130 15.400 1.00 27.94 ATOM 703 CA LEU 1548 −4.017 −0.770 16.223 1.00 26.98 ATOM 704 CB LEU 1548 −3.623 −0.735 17.708 1.00 24.65 ATOM 705 CG LEU 1548 −2.327 −1.450 18.108 1.00 25.38 ATOM 706 CD 1 LEU 1548 −2.189 −1.428 19.613 1.00 25.73 ATOM 707 CD2 LEU 1548 −2.337 −2.886 17.621 1.00 23.92 ATOM 708 C LEU 1548 −5.369 −0.113 16.042 1.00 26.65 ATOM 709 O LEU 1548 −6.392 −0.752 16.238 1.00 27.11 ATOM 710 N GLY 1549 −5.378 1.163 15.684 1.00 25.04 ATOM 712 CA GLY 1549 −6.643 1.855 15.516 1.00 25.47 ATOM 713 C GLY 1549 −6.417 3.336 15.367 1.00 26.23 ATOM 714 O GLY 1549 −5.267 3.781 15.287 1.00 28.41 ATOM 715 N ALA 1550 −7.501 4.104 15.349 1.00 25.49 ATOM 717 CA ALA 1550 −7.408 5.550 15.198 1.00 24.81 ATOM 718 CB ALA 1550 −7.176 5.913 13.724 1.00 21.79 ATOM 719 C ALA 1550 −8.645 6.271 15.691 1.00 25.51 ATOM 720 O ALA 1550 −9.738 5.702 15.726 1.00 24.09 ATOM 721 N CYS 1551 −8.440 7.527 16.080 1.00 24.90 ATOM 723 CA CYS 1551 −9.492 8.438 36.511 1.00 26.80 ATOM 724 CB CYS 1551 −9.243 8.932 17.944 1.00 26.32 ATOM 725 SG CYS 1551 −9.333 7.655 19.223 1.00 32.31 ATOM 726 C CYS 1551 −9.341 9.585 15.502 1.00 28.31 ATOM 727 O CYS 1551 −8.361 10.338 15.537 1.00 28.42 ATOM 728 N THR 1552 −10.261 9.660 14.547 1.00 28.38 ATOM 730 CA THR 1552 −10.198 10.671 13.498 1.00 31.26 ATOM 731 CB THR 1552 −10.159 9.977 12.095 1.00 30.07 ATOM 732 OG1 THR 1552 −11.406 9.309 11.836 1.00 29.64 ATOM 734 CG2 THR 1552 −9.044 8.945 12.053 1.00 28.65 ATOM 735 C THR 1552 −11.355 11.662 13.509 1.00 33.31 ATOM 736 O THR 1552 −11.295 12.722 12.874 1.00 31.94 ATOM 737 N GLN 1553 −12.420 11.309 14.214 1.00 36.09 ATOM 739 CA GLN 1553 −13.598 12.158 14.245 1.00 39.26 ATOM 740 CB GLN 1553 −14.864 11.299 14.145 1.00 36.61 ATOM 741 CG GLN 1553 −14.932 10.436 12.881 1.00 37.72 ATOM 742 CD GLN 1553 −14.762 11.247 11.601 1.00 38.41 ATOM 743 OE1 GLN 1553 −15.491 12.210 11.363 1.00 37.88 ATOM 744 NE2 GLN 1553 −13.798 10.858 10.770 1.00 37.67 ATOM 747 C GLN 1553 −13.671 13.079 15.451 1.00 41.28 ATOM 748 O GLN 1553 −13.150 12.758 16.513 1.00 41.37 ATOM 749 N ASP 1554 −14.282 14.246 15.243 1.00 44.93 ATOM 751 CA ASP 1554 −14.487 15.254 16.281 1.00 48.05 ATOM 752 CB ASP 1554 −15.828 15.009 16.975 1.00 50.80 ATOM 753 CG ASP 1554 −17.007 15.281 16.067 1.00 56.88 ATOM 754 OD1 ASP 1554 −17.921 16.019 16.491 1.00 63.89 ATOM 755 OD2 ASP 1554 −17.016 14.776 14.925 1.00 58.98 ATOM 756 C ASP 1554 −13.367 15.366 17.316 1.00 48.04 ATOM 757 O ASP 1554 −13.556 15.056 18.502 1.00 48.73 ATOM 758 N GLY 1555 −12.205 15.819 16.860 1.00 44.30 ATOM 760 CA GLY 1555 −11.080 15.960 17.756 1.00 42.32 ATOM 761 C GLY 1555 −9.761 15.713 17.052 1.00 40.69 ATOM 762 O GLY 1555 −9.740 15.465 15.848 1.00 40.71 ATOM 763 N PRO 1556 −8.644 15.776 17.782 1.00 39.49 ATOM 764 CD PRO 1556 −8.585 15.983 19.235 1.00 40.36 ATOM 765 CA PRO 1556 −7.298 15.566 17.250 1.00 38.37 ATOM 766 CB PRO 1556 −6.405 15.771 18.470 1.00 38.47 ATOM 767 CG PRO 1556 −7.226 16.573 19.388 1.00 41.77 ATOM 768 C PRO 1556 −7.140 14.154 16.746 1.00 36.92 ATOM 769 O PRO 1556 −7.606 13.208 17.371 1.00 37.04 ATOM 770 N LEU 1557 −6.447 14.017 15.627 1.00 36.70 ATOM 772 CA LEU 1557 −6.201 12.719 15.037 1.00 34.81 ATOM 773 CB LEU 1557 −5.528 12.885 13.664 1.00 32.49 ATOM 774 CG LEU 1557 −5.004 11.623 12.954 1.00 30.83 ATOM 775 CD1 LEU 1557 −6.146 10.655 12.664 1.00 26.28 ATOM 776 CD2 LEU 1557 −4.283 12.014 11.672 1.00 25.55 ATOM 777 C LEU 1557 −5.290 11.925 15.961 1.00 33.63 ATOM 778 O LEU 1557 −4.229 12.410 16.369 1.00 33.62 ATOM 779 N TYR 1558 −5.718 10.724 16.319 1.00 31.97 ATOM 781 CA TYR 1558 −4.902 9.863 17.147 1.00 31.81 ATOM 782 CB TYR 1558 −5.614 9.500 18.462 1.00 33.55 ATOM 783 CG TYR 1558 −5.710 10.638 19.461 1.00 35.33 ATOM 784 CD1 TYR 1558 −6.644 10.608 20.499 1.00 35.68 ATOM 785 CE1 TYR 1558 −6.757 11.670 21.394 1.00 38.60 ATOM 786 CD2 TYR 1558 −4.883 11.759 19.349 1.00 38.62 ATOM 787 CE2 TYR 1558 −4.985 12.824 20.235 1.00 40.33 ATOM 788 CZ TYR 1558 −5.924 12.781 21.254 1.00 41.70 ATOM 789 OH TYR 1558 −6.040 13.867 22.104 1.00 42.66 ATOM 791 C TYR 1558 −4.607 8.604 16.345 1.00 31.08 ATOM 792 O TYR 1558 −5.527 7.937 15.857 1.00 31.28 ATOM 793 N VAL 1559 −3.328 8.336 16.116 1.00 28.34 ATOM 795 CA VAL 1559 −2.934 7.132 15.403 1.00 26.39 ATOM 796 CB VAL 1559 −1.830 7.401 14.364 1.00 29.17 ATOM 797 CG1 VAL 1559 −1.463 6.103 13.648 1.00 26.25 ATOM 798 CG2 VAL 1559 −2.297 8.461 13.360 1.00 29.56 ATOM 799 C VAL 1559 −2.411 6.226 16.498 1.00 25.14 ATOM 800 O VAL 1559 −1.396 6.522 17.120 1.00 28.04 ATOM 801 N ILE 1560 −3.164 5.171 16.783 1.00 25.28 ATOM 803 CA ILE 1560 −2.832 4.208 17.831 1.00 24.81 ATOM 804 CB ILE 1560 −4.133 3.669 18.496 1.00 24.63 ATOM 805 CG2 ILE 1560 −3.790 2.812 19.728 1.00 20.93 ATOM 806 CG1 ILE 1560 −5.044 4.854 18.869 1.00 22.94 ATOM 807 CD1 ILE 1560 −6.499 4.502 19.028 1.00 25.34 ATOM 808 C ILE 1560 −1.994 3.051 17.286 1.00 26.38 ATOM 809 O ILE 1560 −2.429 2.301 16.398 1.00 26.14 ATOM 810 N VAL 1561 −0.782 2.911 17.809 1.00 27.31 ATOM 812 CA VAL 1561 0.112 1.852 17.359 1.00 27.32 ATOM 813 CB VAL 1561 1.309 2.435 16.527 1.00 25.01 ATOM 814 CG1 VAL 1561 0.785 3.220 15.338 1.00 19.39 ATOM 815 CG2 VAL 1561 2.370 3.340 17.397 1.00 26.08 ATOM 816 C VAL 1561 0.615 1.029 18.548 1.00 25.89 ATOM 817 O VAL 1561 0.364 1.373 19.713 1.00 25.64 ATOM 818 N GLU 1562 1.288 −0.076 18.250 1.00 24.49 ATOM 820 CA GLU 1562 1.806 −0.949 19.284 1.00 25.00 ATOM 821 CB GLU 1562 2.357 −2.231 18.677 1.00 23.69 ATOM 822 CG GLU 1562 1.272 −3.170 18.219 1.00 24.29 ATOM 823 CD GLU 1562 1.814 −4.393 17.514 1.00 27.65 ATOM 824 OE1 GLU 1562 1.218 −5.480 17.649 1.00 29.50 ATOM 825 OE2 GLU 1562 2.832 −4.270 16.807 1.00 32.34 ATOM 826 C GLU 1562 2.840 −0.279 20.170 1.00 27.27 ATOM 827 O GLU 1562 3.596 0.576 19.729 1.00 26.18 ATOM 828 N TYR 1563 2.822 −0.663 21.441 1.00 30.39 ATOM 830 CA TYR 1563 3.715 −0.121 22.454 1.00 32.48 ATOM 831 CB TYR 1563 2.932 0.132 23.750 1.00 33.91 ATOM 832 CG TYR 1563 3.788 0.535 24.928 1.00 34.93 ATOM 833 CD1 TYR 1563 4.606 1.664 24.871 1.00 34.50 ATOM 834 CE1 TYR 1563 5.374 2.051 25.967 1.00 37.77 ATOM 835 CD2 TYR 1563 3.758 −0.201 26.108 1.00 33.54 ATOM 836 CE2 TYR 1563 4.519 0.171 27.205 1.00 34.94 ATOM 837 CZ TYR 1563 5.321 1.296 27.128 1.00 37.22 ATOM 838 OH TYR 1563 6.087 1.648 28.206 1.00 45.36 ATOM 840 C TYR 1563 4.896 −1.039 22.730 1.00 31.53 ATOM 841 O TYR 1563 4.737 −2.252 22.895 1.00 30.43 ATOM 842 N ALA 1564 6.082 −0.444 22.761 1.00 32.28 ATOM 844 CA ALA 1564 7.326 −1.167 23.026 1.00 32.59 ATOM 845 CB ALA 1564 8.308 −0.957 21.863 1.00 30.11 ATOM 846 C ALA 1564 7.897 −0.608 24.334 1.00 31.81 ATOM 847 O ALA 1564 8.563 0.427 24.345 1.00 34.11 ATOM 848 N SER 1565 7.619 −1.296 25.434 1.00 34.09 ATOM 850 CA SER 1565 8.039 −0.853 26.763 1.00 35.05 ATOM 851 CB SER 1565 7.400 −1.725 27.829 1.00 30.13 ATOM 852 OG SER 1565 7.689 −3.084 27.579 1.00 38.17 ATOM 854 C SER 1565 9.526 −0.769 27.041 1.00 35.03 ATOM 855 O SER 1565 9.947 −0.001 27.902 1.00 37.12 ATOM 856 N LYS 1566 10.321 −1.557 26.330 1.00 34.55 ATOM 858 CA LYS 1566 11.756 −1.559 26.562 1.00 33.48 ATOM 859 CB LYS 1566 12.291 −2.990 26.508 1.00 31.90 ATOM 860 CG LYS 1566 11.674 −3.865 27.586 1.00 28.63 ATOM 861 CD LYS 1566 12.162 −5.287 27.508 1.00 34.97 ATOM 862 CE LYS 1566 11.763 −6.042 28.761 1.00 36.82 ATOM 863 NZ LYS 1566 12.288 −7.433 28.748 1.00 41.32 ATOM 867 C LYS 1566 12.567 −0.613 25.691 1.00 34.98 ATOM 868 O LYS 1566 13.785 −0.740 25.607 1.00 38.03 ATOM 869 N GLY 1567 11.892 0.338 25.049 1.00 36.00 ATOM 871 CA GLY 1567 12.582 1.322 24.222 1.00 34.14 ATOM 872 C GLY 1567 13.245 0.864 22.933 1.00 32.01 ATOM 873 O GLY 1567 12.975 −0.222 22.439 1.00 31.95 ATOM 874 N ASN 1568 14.091 1.719 22.360 1.00 33.51 ATOM 876 CA ASN 1568 14.774 1.375 21.121 1.00 34.20 ATOM 877 CB ASN 1568 15.203 2.627 20.332 1.00 34.07 ATOM 878 CG ASN 1568 16.420 3.321 20.910 1.00 35.09 ATOM 879 OD1 ASM 1568 17.453 2.709 21.156 1.00 34.36 ATOM 880 ND2 ASN 1568 16.317 4.624 21.066 1.00 38.38 ATOM 883 C ASN 1568 15.927 0.401 21.325 1.00 33.38 ATOM 884 O ASN 1568 16.490 0.315 22.414 1.00 34.93 ATOM 885 N LEU 1569 16.276 −0.327 20.263 1.00 31.11 ATOM 887 CA LEU 1569 17.333 −1.316 20.298 1.00 30.44 ATOM 888 CB LEU 1569 17.437 −2.008 18.928 1.00 29.46 ATOM 889 CG LEU 1569 18.438 −3.148 18.741 1.00 29.01 ATOM 890 CD1 LEU 1569 18.285 −4.219 19.840 1.00 28.81 ATOM 891 CD2 LEU 1569 18.263 −3.740 17.338 1.00 26.62 ATOM 892 C LEU 1569 18.706 −0.805 20.762 1.00 30.16 ATOM 893 O LEU 1569 19.400 −1.501 21.496 1.00 27.32 ATOM 894 N ARG 1570 19.097 0.396 20.344 1.00 30.74 ATOM 896 CA ARG 1570 20.386 0.951 20.758 1.00 33.72 ATOM 897 CB ARG 1570 20.597 2.349 20.160 1.00 32.82 ATOM 898 CG ARG 1570 21.873 3.009 20.662 1.00 36.90 ATOM 899 CD ARG 1570 21.966 4.481 20.332 1.00 39.32 ATOM 900 NE ARG 1570 20.749 5.222 20.664 1.00 50.32 ATOM 902 CZ ARG 1570 20.376 5.600 21.889 1.00 51.90 ATOM 903 NH1 ARG 1570 21.118 5.316 22.960 1.00 50.15 ATOM 906 NH2 ARG 1570 19.246 6.284 22.033 1.00 53.67 ATOM 909 C ARG 1570 20.434 1.022 22.298 1.00 35.75 ATOM 910 O ARG 1570 21.324 0.444 22.939 1.00 35.67 ATOM 911 N GLU 1571 19.444 1.695 22.880 1.00 35.56 ATOM 913 CA GLU 1571 19.331 1.835 24.328 1.00 36.50 ATOM 914 CB GLU 1571 18.055 2.607 24.667 1.00 39.08 ATOM 915 CG GLU 1571 le.061 4.056 24.208 1.00 46.75 ATOM 916 CD GLU 1571 16.694 4.721 24.311 1.00 51.36 ATOM 917 OE1 GLU 1571 15.676 3.996 24.417 1.00 55.22 ATOM 918 OE2 GLU 1571 16.635 5.972 24.267 1.00 53.59 ATOM 919 C GLU 1571 19.314 0.469 25.022 1.00 34.82 ATOM 920 O GLU 1571 20.018 0.242 26.013 1.00 35.05 ATOM 921 N TYR 1572 18.520 −0.441 24.469 1.00 33.35 ATOM 923 CA TYR 1572 18.366 −1.796 24.986 1.00 31.83 ATOM 924 CB TYR 1572 17.365 −2.544 24.102 1.00 30.77 ATOM 925 CG TYR 1572 17.170 −4.008 24.408 1.00 28.50 ATOM 926 CD1 TYR 1572 16.193 −4.420 25.313 1.00 30.48 ATOM 927 CE1 TYR 1572 15.977 −5.760 25.574 1.00 30.97 ATOM 928 CD2 TYR 1572 17.933 −4.985 23.772 1.00 26.14 ATOM 929 CE2 TYR 1572 17.725 −6.329 24.027 1.00 26.21 ATOM 930 CZ TYR 1572 16.742 −6.708 24.935 1.00 30.30 ATOM 931 OH TYR 1572 16.518 −8.042 25.214 1.00 33.52 ATOM 933 C TYR 1572 19.692 −2.556 25.044 1.00 34.83 ATOM 934 O TYR 1572 19.959 −3.308 25.992 1.00 34.93 ATOM 935 N LEU 1573 20.517 −2.370 24.020 1.00 34.34 ATOM 937 CA LEU 1573 21.803 −3.053 23.961 1.00 35.38 ATOM 938 CB LEU 1573 22.357 −3.027 22.531 1.00 32.71 ATOM 939 CG LEU 1573 21.669 −3.891 21.464 1.00 29.16 ATOM 940 CD1 LEU 1573 22.161 −3.503 20.087 1.00 26.98 ATOM 941 CD2 LEU 1573 21.932 −5.351 21.710 1.00 28.85 ATOM 942 C LEU 1573 22.799 −2.420 24.933 1.00 37.54 ATOM 943 O LEU 1573 23.511 −3.123 25.659 1.00 36.67 ATOM 944 N GLN 1574 22.814 −1.092 24.969 1.00 37.90 ATOM 946 CA GLN 1574 23.729 −0.368 25.838 1.00 39.77 ATOM 947 CB GLN 1574 23.624 1.138 25.572 1.00 40.09 ATOM 948 CG GLN 1574 24.208 1.549 24.217 1.00 42.28 ATOM 949 CD GLN 1574 24.030 3.018 23.896 1.00 44.28 ATOM 950 OE1 GLN 1574 23.362 3.755 24.615 1.00 47.55 ATOM 951 NE2 GLN 1574 24.613 3.448 22.790 1.00 46.09 ATOM 954 C GLN 1574 23.490 −0.697 27.310 1.00 40.75 ATOM 955 O GLN 1574 24.440 −0.939 28.059 1.00 41.29 ATOM 956 N ALA 1575 22.220 −0.783 27.696 1.00 40.10 ATOM 958 CA ALA 1575 21.842 −1.088 29.069 1.00 38.81 ATOM 959 CB ALA 1575 20.349 −0.819 29.273 1.00 35.69 ATOM 960 C ALA 1575 22.192 −2.514 29.503 1.00 40.63 ATOM 961 O ALA 1575 22.098 −2.843 30.690 1.00 43.39 ATOM 962 N ARG 1576 22.602 −3.357 28.561 1.00 38.39 ATOM 964 CA ARG 1576 22.945 −4.729 28.896 1.00 37.69 ATOM 965 CB ARG 1576 22.034 −5.689 28.137 1.00 38.16 ATOM 966 CG ARG 1576 20.594 −5.547 28.589 1.00 37.89 ATOM 967 CD ARG 1576 19.622 −6.281 27.711 1.00 37.36 ATOM 968 NE ARG 1576 18.267 −6.255 28.265 1.00 34.99 ATOM 970 CZ ARG 1576 17.565 −5.150 28.484 1.00 36.94 ATOM 971 NH1 ARG 1576 18.083 −3.960 28.209 1.00 36.18 ATOM 974 NH2 ARG 1576 16.310 −5.237 28.909 1.00 40.93 ATOM 977 C ARG 1576 24.413 −5.073 28.704 1.00 38.93 ATOM 978 O ARG 1576 24.801 −6.249 28.699 1.00 39.75 ATOM 979 N ARG 1577 25.233 −4.036 28.570 1.00 39.21 ATOM 981 CA ARG 1577 26.671 −4.196 28.413 1.00 38.97 ATOM 982 CB ARG 1577 27.307 −2.870 28.000 1.00 36.06 ATOM 983 CG ARG 1577 26.992 −2.408 26.610 1.00 36.41 ATOM 984 CD ARG 1577 27.695 −1.094 26.337 1.00 36.17 ATOM 985 NE ARG 1577 27.776 −0.806 24.907 1.00 38.45 ATOM 987 CZ ARG 1577 28.284 0.309 24.387 1.00 39.00 ATOM 988 NH1 ARG 1577 28.764 1.262 25.175 1.00 38.88 ATOM 991 NH2 ARG 1577 28.311 0.469 23.071 1.00 37.76 ATOM 994 C ARG 1577 27.247 −4.571 29.772 1.00 40.59 ATOM 995 O ARG 1577 26.680 −4.217 30.800 1.00 38.52 ATOM 996 N PRO 1578 28.358 −5.327 29.796 1.00 43.19 ATOM 997 CD PRO 1578 29.077 −5.980 28.692 1.00 44.84 ATOM 998 CA PRO 1578 28.952 −5.692 31.088 1.00 45.06 ATOM 999 CB PRO 1578 30.065 −6.673 30.689 1.00 44.86 ATOM 1000 CG PRO 1578 30.431 −6.229 29.308 1.00 44.56 ATOM 1001 C PRO 1578 29.513 −4.420 31.734 1.00 44.93 ATOM 1002 O PRO 1578 29.809 −3.439 31.043 1.00 43.13 ATOM 1003 N PRO 1579 29.649 −4.414 33.067 1.00 47.61 ATOM 1004 CD PRO 1579 29.315 −5.492 34.012 1.00 48.39 ATOM 1005 CA PRO 1579 30.173 −3.247 33.784 1.00 48.74 ATOM 1006 CB PRO 1579 30.138 −3.706 35.238 1.00 49.73 ATOM 1007 CG PRO 1579 29.027 −4.711 35.259 1.00 49.21 ATOM 1008 C PRO 1579 31.591 −2.888 33.357 1.00 49.67 ATOM 1009 O PRO 1579 32.483 −3.733 33.361 1.00 52.07 ATOM 1010 N GLU 1592 19.165 −5.411 32.444 1.00 64.83 ATOM 1012 CA GLU 1592 20.603 −5.147 32.491 1.00 64.82 ATOM 1013 CB GLU 1592 20.969 −4.421 33.784 1.00 67.61 ATOM 1014 C GLU 1592 21.448 −6.413 32.335 1.00 63.99 ATOM 1015 O GLU 1592 22.653 −6.336 32.098 1.00 65.67 ATOM 1016 N GLU 1593 20.821 −7.575 32.485 1.00 62.41 ATOM 1018 CA GLU 1593 21.534 −8.844 32.342 1.00 61.23 ATOM 1019 CS GLU 1593 20.595 −10.017 32.600 1.00 61.20 ATOM 1020 C GLU 1593 22.141 −8.953 30.944 1.00 59.26 ATOM 1021 O GLU 1593 21.494 −8.631 29.945 1.00 59.84 ATOM 1022 N GLN 1594 23.388 −9.405 30.888 1.00 57.94 ATOM 1024 CA GLN 1594 24.101 −9.558 29.625 1.00 54.91 ATOM 1025 CB GLN 1594 25.501 −10.141 29.865 1.00 55.13 ATOM 1026 CG GLN 1594 26.439 −9.252 30.679 1.00 56.93 ATOM 1027 CD GLN 1594 27.682 −9.997 31.180 1.00 59.60 ATOM 1028 OE1 GLN 1594 28.241 −10.858 30.488 1.00 58.45 ATOM 1029 NE2 GLN 1594 28.117 −9.662 32.393 1.00 58.95 ATOM 1032 C GLN 1594 23.331 −10.438 28.640 1.00 52.30 ATOM 1033 O GLN 1594 22.637 −11.389 29.025 1.00 52.03 ATOM 1034 N LEU 1595 23.438 −10.091 27.366 1.00 49.60 ATOM 1036 CA LEU 1595 22.782 −10.836 26.308 1.00 45.16 ATOM 1037 CB LEU 1595 22.459 −9.907 25.135 1.00 41.36 ATOM 1038 CG LEU 1595 21.463 −8.815 25.523 1.00 39.43 ATOM 1039 CD1 LEU 1595 21.617 −7.583 24.644 1.00 36.21 ATOM 1040 CD2 LEU 1595 20.060 −9.389 25.480 1.00 34.91 ATOM 1041 C LEU 1595 23.747 −11.900 25.858 1.00 43.30 ATOM 1042 O LEU 1595 24.953 −11.675 25.841 1.00 43.62 ATOM 1043 N SER 1596 23.230 −13.081 25.553 1.00 42.92 ATOM 1045 CA SER 1596 24.085 −14.150 25.077 1.00 41.86 ATOM 1046 CB SER 1596 23.410 −15.502 25.298 1.00 40.86 ATOM 1047 OG SER 1596 22.188 −15.596 24.595 1.00 37.88 ATOM 1049 C SER 1596 24.322 −13.914 23.587 1.00 41.59 ATOM 1050 O SER 1596 23.657 −13.077 22.966 1.00 41.94 ATOM 1051 N SER 1597 25.275 −14.637 23.018 1.00 39.60 ATOM 1053 CA SER 1597 25.557 −14.518 21.603 1.00 39.74 ATOM 1054 CB SER 1597 26.729 −15.409 21.223 1.00 41.38 ATOM 1055 OG SER 1597 27.824 −15.147 22.077 1.00 50.59 ATOM 1057 C SER 1597 24.315 −14.921 20.818 1.00 38.16 ATOM 1058 O SER 1597 24.036 −14.353 19.769 1.00 38.03 ATOM 1059 N LYS 1598 23.560 −15.891 21.327 1.00 36.40 ATOM 1061 CA LYS 1598 22.362 −16.312 20.634 1.00 35.97 ATOM 1062 CB LYS 1598 21.791 −17.594 21.228 1.00 36.69 ATOM 1063 CG LYS 1598 20.989 −18.402 20.198 1.00 40.42 ATOM 1064 CD LYS 1598 20.164 −19.499 20.838 1.00 40.37 ATOM 1065 CE LYS 1598 19.792 −20.572 19.829 1.00 46.34 ATOM 1066 NZ LYS 1598 20.993 −21.338 19.362 1.00 45.29 ATOM 1070 C LYS 1598 21.324 −15.194 20.696 1.00 37.49 ATOM 1071 O LYS 1598 20.567 −14.983 19.738 1.00 38.10 ATOM 1072 N ASP 1599 21.316 −14.458 21.807 1.00 35.21 ATOM 1074 CA ASP 1599 20.380 −13.352 21.983 1.00 34.02 ATOM 1075 CB ASP 1599 20.556 −12.686 23.346 1.00 37.78 ATOM 1076 CG ASP 1599 19.970 −13.493 24.483 1.00 40.05 ATOM 1077 OD1 ASP 1599 20.270 −13.143 25.642 1.00 42.73 ATOM 1078 OD2 ASP 1599 19.204 −14.450 24.235 1.00 42.39 ATOM 1079 C ASP 1599 20.633 −12.306 20.922 1.00 32.84 ATOM 1080 O ASP 1599 19.694 −11.779 20.311 1.00 30.59 ATOM 1081 N LEU 1600 21.912 −11.999 20.724 1.00 31.11 ATOM 1083 CA LEU 1600 22.323 −10.998 19.744 1.00 32.17 ATOM 1084 CB LEU 1600 23.823 −10.722 19.875 1.00 32.30 ATOM 1085 CG LEU 1600 24.275 −10.162 21.235 1.00 31.08 ATOM 1086 CD1 LEU 1600 25.794 −9.931 21.242 1.00 30.59 ATOM 1087 CD2 LEU 1600 23.549 −8.863 21.514 1.00 28.89 ATOM 1088 C LEU 1600 21.949 −11.390 18.311 1.00 30.77 ATOM 1089 O LEU 1600 21.352 −10.601 17.574 1.00 29.87 ATOM 1090 N VAL 1601 22.269 −12.623 17.933 1.00 30.19 ATOM 1092 CA VAL 1601 21.954 −13.115 16.602 1.00 29.25 ATOM 1093 CB VAL 1601 22.593 −14.497 16.349 1.00 31.27 ATOM 1094 CG1 VAL 1601 22.355 −14.936 14.914 1.00 31.60 ATOM 1095 CG2 VAL 1601 24.093 −14.434 16.622 1.00 31.91 ATOM 1096 C VAL 1601 20.438 −13.181 16.405 1.00 29.06 ATOM 1097 O VAL 1601 19.946 −12.914 15.310 1.00 27.71 ATOM 1098 N SER 1602 19.702 −13.511 17.468 1.00 29.10 ATOM 1100 CA SER 1602 18.243 −13.585 17.400 1.00 29.29 ATOM 1101 CB SER 1602 17.680 −14.189 18.679 1.00 30.81 ATOM 1102 OG SER 1602 16.266 −14.074 18.692 1.00 35.78 ATOM 1104 C SER 1602 17.649 −12.199 17.156 1.00 28.98 ATOM 1105 O SER 1602 16.662 −12.039 16.426 1.00 26.82 ATOM 1106 N CYS 1603 18.274 −11.202 17.765 1.00 29.06 ATOM 1108 CA CYS 1603 17.870 −9.823 17.599 1.00 29.22 ATOM 1109 CB CYS 1603 18.784 −8.943 18.438 1.00 29.66 ATOM 1110 SG CYS 1603 18.575 −7.212 18.103 0.50 23.69 PRT1 ATOM 1111 C CYS 1603 17.988 −9.422 16.112 1.00 29.23 ATOM 1112 O CYS 1603 17.087 −8.796 15.552 1.00 27.52 ATOM 1113 N ALA 1604 19.113 −9.778 15.491 1.00 27.87 ATOM 1115 CA ALA 1604 19.376 −9.484 14.077 1.00 26.37 ATOM 1116 CB ALA 1604 20.783 −9.941 13.690 1.00 23.88 ATOM 1117 C ALA 1604 18.349 −10.203 13.223 1.00 25.82 ATOM 1118 O ALA 1604 37.788 −9.631 12.289 1.00 25.84 ATOM 1119 N TYR 1605 18.119 −11.468 13.544 1.00 25.56 ATOM 1121 CA TYR 1605 17.152 −12.276 12.827 1.00 27.81 ATOM 1122 CB TYR 1605 17.080 −13.662 13.456 1.00 26.66 ATOM 1123 CG TYR 1605 15.974 −14.515 12.886 1.00 30.75 ATOM 1124 CD1 TYR 1605 16.111 −15.141 11.640 1.00 30.20 ATOM 1125 CE1 TYR 1605 15.088 −15.944 11.126 1.00 30.03 ATOM 1126 CD2 TYR 1605 14.790 −14.707 13.596 1.00 30.73 ATOM 1127 CE2 TYR 1605 13.775 −15.500 13.097 1.00 30.71 ATOM 1128 CZ TYR 1605 13.930 −16.117 11.867 1.00 30.93 ATOM 1129 OH TYR 1605 12.923 −16.928 11.417 1.00 32.31 ATOM 1131 C TYR 1605 15.748 −11.641 12.775 1.00 26.15 ATOM 1132 O TYR 1605 15.147 −11.551 11.702 1.00 26.64 ATOM 1133 N GLN 1606 15.244 −11.200 13.926 1.00 25.48 ATOM 1135 CA GLN 1606 13.921 −10.581 14.023 1.00 26.86 ATOM 1136 CB GLN 1606 13.589 −10.269 15.482 1.00 26.83 ATOM 1137 CG GLN 1606 13.357 −11.508 16.332 1.00 25.84 ATOM 1138 CD GLN 1606 13.151 −11.167 17.791 1.00 30.86 ATOM 1139 OE1 GLN 1606 12.202 −10.471 18.150 1.00 31.87 ATOM 1140 NE2 GLN 1606 14.056 −11.631 18.640 1.00 31.67 ATOM 1143 C GLN 1606 13.835 −9.310 13.186 1.00 27.52 ATOM 1144 O GLN 1606 12.831 −9.058 12.506 1.00 26.05 ATOM 1145 N VAL 1607 14.904 −8.523 13.216 1.00 26.68 ATOM 1147 CA VAL 1607 14.963 −7.301 12.435 1.00 25.66 ATOM 1148 CB VAL 1607 16.225 −6.485 12.787 1.00 28.50 ATOM 1149 CG1 VAL 1607 16.363 −5.274 11.853 1.00 26.04 ATOM 1150 CG2 VAL 1607 16.151 −6.031 14.246 1.00 24.45 ATOM 1151 C VAL 1607 14.934 −7.641 10.938 1.00 24.89 ATOM 1152 O VAL 1607 14.184 −7.033 10.177 1.00 25.86 ATOM 1153 N ALA 1608 15.738 −8.619 10.522 1.00 25.24 ATOM 1155 CA ALA 1608 15.773 −9.039 9.120 1.00 22.95 ATOM 1156 CB ALA 1608 16.813 −10.117 8.920 1.00 20.24 ATOM 1157 C ALA 1608 14.383 −9.541 8.679 1.00 25.71 ATOM 1158 O ALA 1608 13.963 −9.319 7.532 1.00 27.48 ATOM 1159 N ARG 1609 13.676 −10.216 9.585 1.00 27.10 ATOM 1161 CA ARG 1609 12.327 −10.708 9.301 1.00 28.55 ATOM 1162 CB ARG 1609 11.840 −11.640 10.397 1.00 31.53 ATOM 1163 CG ARG 1609 12.407 −13.005 10.290 1.00 36.05 ATOM 1164 CD ARG 1609 11.537 −13.931 11.056 1.00 40.28 ATOM 1165 NE ARG 1609 10.849 −14.874 10.190 1.00 42.06 ATOM 1167 CZ ARG 1609 9.974 −15.771 10.632 1.00 42.08 ATOM 1168 NH1 ARG 1609 9.678 −15.834 11.928 1.00 40.32 ATOM 1171 NH2 ARG 1609 9.416 −16.620 9.784 1.00 43.27 ATOM 1174 C ARG 1609 11.329 −9.569 9.124 1.00 25.55 ATOM 1175 O ARG 1609 10.469 −9.621 8.231 1.00 26.98 ATOM 1176 N GLY 1610 11.418 −8.565 9.996 1.00 23.92 ATOM 1178 CA GLY 1610 10.555 −7.406 9.870 1.00 22.19 ATOM 1179 C GLY 1610 10.800 −6.747 8.512 1.00 25.92 ATOM 1180 O GLY 1610 9.855 −6.424 7.772 1.00 23.49 ATOM 1181 N MET 1611 12.076 −6.589 8.163 1.00 23.15 ATOM 1183 CA MET 1611 12.456 −5.989 6.888 1.00 22.57 ATOM 1184 CB MET 1611 13.956 −5.710 6.849 1.00 22.18 ATOM 1185 CG MET 1611 14.398 −4.542 7.729 1.00 22.63 ATOM 1186 SD NET 1611 13.478 −3.006 7.426 1.00 25.23 ATOM 1187 CE MET 1611 13.812 −2.688 5.675 1.00 21.38 ATOM 1188 C MET 1611 12.050 −6.848 5.681 1.00 23.96 ATOM 1189 O MET 1611 11.673 −6.326 4.633 1.00 25.26 ATOM 1190 N GLU 1612 12.130 −8.163 5.822 1.00 24.34 ATOM 1192 CA GLU 1612 11.755 −9.043 4.733 1.00 25.56 ATOM 1193 CB GLU 1612 12.018 −10.494 5.121 1.00 24.96 ATOM 1194 CG GLU 1612 11.703 −11.488 4.009 1.00 26.79 ATOM 1195 CD GLU 1612 11.812 −12.931 4.450 1.00 26.96 ATOM 1196 OE1 GLU 1612 11.557 −13.212 5.636 1.00 30.98 ATOM 1197 OE2 GLU 1612 12.154 −13.791 3.611 1.00 32.31 ATOM 1198 C GLU 1612 10.267 −8.829 4.415 1.00 25.70 ATOM 1199 O GLU 1612 9.860 −8.753 3.252 1.00 24.30 ATOM 1200 N TYR 1613 9.463 −8.723 5.465 1.00 23.55 ATOM 1202 CA TYR 1613 8.037 −8.501 5.294 1.00 22.94 ATOM 1203 CB TYR 1613 7.314 −8.586 6.650 1.00 24.00 ATOM 1204 CG TYR 1613 5.841 −8.281 6.549 1.00 22.93 ATOM 1205 CD1 TYR 1613 4.945 −9.245 6.097 1.00 21.60 ATOM 1206 CE1 TYR 1613 3.582 −8.962 5.963 1.00 21.14 ATOM 1207 CD2 TYR 1613 5.347 −7.018 6.869 1.00 25.81 ATOM 1208 CE2 TYR 1613 3.979 −6.718 6.733 1.00 24.45 ATOM 1209 CZ TYR 1613 3.112 −7.697 6.281 1.00 23.28 ATOM 1210 OH TYR 1613 1.775 −7.411 6.126 1.00 22.95 ATOM 1212 C TYR 1613 7.803 −7.138 4.637 1.00 22.57 ATOM 1213 O TYR 1613 7.022 −7.024 3.699 1.00 24.72 ATOM 1214 N LEU 1614 8.460 −6.101 5.156 1.00 22.16 ATOM 1216 CA LEU 1614 8.334 −4.755 4.615 1.00 22.60 ATOM 1217 CB LEU 1614 9.175 −3.772 5.440 1.00 22.56 ATOM 1218 CG LEU 1614 8.577 −3.415 6.802 1.00 24.92 ATOM 1219 CD1 LEU 1614 9.535 −2.541 7.580 1.00 21.46 ATOM 1220 CD2 LEU 1614 7.218 −2.711 6.611 1.00 21.87 ATOM 1221 C LEU 1614 8.699 −4.683 3.124 1.00 23.76 ATOM 1222 O LEU 1614 7.975 −4.077 2.326 1.00 23.84 ATOM 1223 N ALA 1615 9.809 −5.314 2.744 1.00 23.48 ATOM 1225 CA ALA 1615 10.232 −5.340 1.352 1.00 22.70 ATOM 1226 CB ALA 1615 11.591 −6.019 1.215 1.00 21.52 ATOM 1227 C ALA 1615 9.188 −6.063 0.505 1.00 22.87 ATOM 1228 O ALA 1615 8.854 −5.591 −0.581 1.00 24.23 ATOM 1229 N SER 1616 8.652 −7.176 1.015 1.00 22.76 ATOM 1231 CA SER 1616 7.638 −7.954 0.295 1.00 22.88 ATOM 1232 CB SER 1616 7.315 −9.251 1.039 1.00 21.39 ATOM 1233 OG SER 1616 6.400 −9.036 2.102 1.00 26.24 ATOM 1235 C SER 1616 6.360 −7.131 0.044 1.00 24.88 ATOM 1236 O SER 1616 5.635 −7.358 −0.927 1.00 24.73 ATOM 1237 N LYS 1617 6.104 −6.173 0.927 1.00 23.82 ATOM 1239 CA LYS 1617 4.970 −5.287 0.810 1.00 22.47 ATOM 1240 CB LYS 1617 4.455 −4.914 2.199 1.00 23.62 ATOM 1241 CG LYS 1617 3.792 −6.072 2.927 1.00 27.16 ATOM 1242 CD LYS 1617 2.551 −6.487 2.169 1.00 30.84 ATOM 1243 CE LYS 1617 1.810 −7.602 2.852 1.00 33.57 ATOM 1244 NZ LYS 1617 2.484 −8.894 2.653 1.00 44.30 ATOM 1248 C LYS 1617 5.346 −4.034 0.035 1.00 23.56 ATOM 1249 O LYS 1617 4.639 −3.030 0.091 1.00 25.16 ATOM 1250 N LYS 1618 6.495 −4.066 −0.638 1.00 24.69 ATOM 1252 CA LYS 1618 6.953 −2.943 −1.468 1.00 24.04 ATOM 1253 CB LYS 1618 5.863 −2.581 −2.492 1.00 26.96 ATOM 1254 CG LYS 1618 5.775 −3.491 −3.709 1.00 29.14 ATOM 1255 CD LYS 1618 5.567 −4.942 −3.345 1.00 33.91 ATOM 1256 CE LYS 1618 5.662 −5.858 −4.558 1.00 32.98 ATOM 1257 NZ LYS 1618 4.431 −5.821 −5.380 1.00 36.73 ATOM 1261 C LYS 1618 7.406 −1.686 −0.713 1.00 24.01 ATOM 1262 O LYS 1618 7.557 −0.606 −1.302 1.00 23.73 ATOM 1263 N CYS 1619 7.689 −1.842 0.573 1.00 25.91 ATOM 1265 CA CYS 1619 8.108 −0.731 1.418 1.00 25.65 ATOM 1266 CB CYS 1619 7.444 −0.885 2.792 1.00 24.93 ATOM 1267 SG CYS 1619 7.941 0.313 4.064 1.00 28.14 ATOM 1268 C CYS 1619 9.631 −0.628 1.573 1.00 23.07 ATOM 1269 O CYS 1619 10.304 −1.630 1.809 1.00 20.98 ATOM 1270 N ILE 1620 10.170 0.573 1.363 1.00 22.95 ATOM 1272 CA ILE 1620 11.604 0.841 1.524 1.00 23.81 ATOM 1273 CB ILE 1620 12.202 1.607 0.276 1.00 24.36 ATOM 1274 CG2 ILE 1620 13.670 1.995 0.506 1.00 17.24 ATOM 1275 CG1 ILE 1620 12.108 0.739 −0.987 1.00 23.13 ATOM 1276 CD1 ILE 1620 12.171 1.544 −2.286 1.00 25.37 ATOM 1277 C ILE 1620 11.633 1.729 2.771 1.00 24.70 ATOM 1278 O ILE 1620 10.981 2.763 2.806 1.00 25.21 ATOM 1279 N HIS 1621 12.348 1.297 3.804 1.00 25.62 ATOM 1281 CA HIS 1621 12.427 2.041 5.057 1.00 25.53 ATOM 1282 CB HIS 1621 13.181 1.237 6.132 1.00 22.76 ATOM 1283 CG HIS 1621 13.004 1.773 7.528 1.00 26.42 ATOM 1284 CD2 HIS 1621 12.356 1.260 8.601 1.00 24.74 ATOM 1285 ND1 HIS 1621 13.474 3.011 7.927 1.00 26.62 ATOM 1287 CE1 HIS 1621 13.119 3.233 9.179 1.00 25.70 ATOM 1288 NE2 HIS 1621 12.439 2.187 9.616 1.00 26.23 ATOM 1290 C HIS 1621 13.073 3.401 4.914 1.00 26.36 ATOM 1291 O HIS 1621 12.528 4.405 5.370 1.00 25.89 ATOM 1292 N ARG 1622 14.271 3.406 4.341 1.00 25.35 ATOM 1294 CA ARG 1622 15.082 4.608 4.140 1.00 25.05 ATOM 1295 CB ARG 1622 14.268 5.766 3.540 1.00 20.89 ATOM 1296 CG ARG 1622 13.709 5.444 2.175 1.00 19.03 ATOM 1297 CD ARG 1622 13.089 6.656 1.488 0.50 14.06 ATOM 1298 NE ARG 1622 12.684 6.300 0.131 0.50 11.96 ATOM 1300 CZ ARG 1622 11.606 5.577 −0.166 0.50 11.83 ATOM 1301 NH1 ARG 1622 10.801 5.137 0.797 0.50 10.20 ATOM 1304 NH2 ARG 1622 11.366 5.239 −3.425 0.50 8.63 ATOM 1307 C ARG 1622 15.877 5.058 5.379 1.00 24.37 ATOM 1308 O ARG 1622 16.787 5.863 5.268 1.00 25.17 ATOM 1309 N ASP 1623 15.555 4.527 6.552 1.00 24.61 ATOM 1311 CA ASP 1623 16.315 4.899 7.748 1.00 28.82 ATOM 1312 CB ASP 1623 15.777 6.173 8.410 1.00 32.33 ATOM 1313 CG ASP 1623 16.733 6.735 9.469 1.00 36.67 ATOM 1314 OD1 ASP 1623 16.276 7.520 10.321 1.00 43.56 ATOM 1315 OD2 ASP 1623 17.937 6.385 9.463 1.00 36.29 ATOM 1316 C ASP 1623 16.408 3.766 8.766 1.00 28.22 ATOM 1317 O ASP 1623 16.118 3.937 9.956 1.00 26.87 ATOM 1318 N LEU 1624 16.783 2.592 8.278 1.00 26.34 ATOM 1320 CA LEU 1624 16.941 1.428 9.132 1.00 26.59 ATOM 1321 CB LEU 1624 16.996 0.168 8.265 1.00 24.59 ATOM 1322 CG LEU 1624 17.082 −1.175 8.978 1.00 24.72 ATOM 1323 CD1 LEU 1624 15.844 −1.408 9.856 1.00 24.35 ATOM 1324 CD2 LEU 1624 17.258 −2.261 7.931 1.00 24.63 ATOM 1325 C LEU 1624 18.210 1.595 10.004 1.00 26.87 ATOM 1326 O LEU 1624 19.322 1.777 9.497 1.00 28.19 ATOM 1327 N ALA 1625 18.009 1.570 11.317 1.00 27.77 ATOM 1329 CA ALA 1625 19.069 1.741 12.309 1.00 24.54 ATOM 1330 CB ALA 1625 19.355 3.210 12.494 1.00 19.81 ATOM 1331 C ALA 1625 18.498 1.173 13.592 1.00 26.44 ATOM 1332 O ALA 1625 17.289 0.961 13.679 1.00 27.58 ATOM 1333 N ALA 1626 19.342 0.940 14.594 1.00 25.38 ATOM 1335 CA ALA 1626 18.872 0.397 15.865 1.00 24.65 ATOM 1336 CB ALA 1626 20.054 0.023 16.774 1.00 23.35 ATOM 1337 C ALA 1626 17.929 1.373 16.578 1.00 25.54 ATOM 1338 O ALA 1626 17.057 0.951 17.325 1.00 27.70 ATOM 1339 N ARG 1627 18.104 2.671 16.344 1.00 25.06 ATOM 1341 CA ARG 1627 17.242 3.675 16.959 1.00 25.48 ATOM 1342 CB ARG 1627 17.706 5.089 16.597 1.00 28.15 ATOM 1343 CG ARG 1627 17.759 5.370 15.084 1.00 33.13 ATOM 1344 CD ARG 1627 18.157 6.811 14.774 1.00 33.29 ATOM 1345 NE ARG 1627 18.442 7.011 13.351 1.00 35.74 ATOM 1347 CZ ARG 1627 19.652 6.889 12.813 1.00 37.40 ATOM 1348 NH1 ARG 1627 20.695 6.585 13.575 1.00 39.73 ATOM 1351 NH2 ARG 1627 19.817 7.012 11.507 1.00 36.90 ATOM 1354 C ARG 1627 15.812 3.491 16.479 1.00 24.81 ATOM 1355 O ARG 1627 14.871 3.853 17.173 1.00 24.05 ATOM 1356 N ASN 1628 15.667 2.910 15.293 1.00 24.80 ATOM 1358 CA ASN 1628 14.368 2.686 14.685 1.00 25.97 ATOM 1359 CB ASN 1628 14.383 3.132 13.225 1.00 30.08 ATOM 1360 CG ASN 1628 14.417 4.640 13.096 1.00 33.62 ATOM 1361 OD1 ASN 1628 13.775 5.347 13.864 1.00 35.11 ATOM 1362 ND2 ASN 1628 15.212 5.141 12.169 1.00 36.31 ATOM 1365 C ASN 1628 13.802 1.288 14.824 1.00 26.03 ATOM 1366 O ASN 1628 12.951 0.869 14.031 1.00 26.87 ATOM 1367 N VAL 1629 14.330 0.550 15.797 1.00 26.04 ATOM 1369 CA VAL 1629 13.854 −0.783 16.128 1.00 25.09 ATOM 1370 CB VAL 1629 14.924 −1.876 15.959 1.00 27.00 ATOM 1371 CG1 VAL 1629 14.390 −3.197 16.546 1.00 20.99 ATOM 1372 CG2 VAL 1629 15.295 −2.051 14.462 1.00 23.26 ATOM 1373 C VAL 1629 13.504 −0.671 17.600 1.00 27.59 ATOM 1374 O VAL 1629 14.340 −0.285 18.418 1.00 25.81 ATOM 1375 N LEU 1630 12.245 −0.929 17.923 1.00 28.17 ATOM 1377 CA LEU 1630 11.768 −0.845 19.296 1.00 30.20 ATOM 1378 CE LEU 1630 10.445 −0.077 19.332 1.00 30.26 ATOM 1379 CG LEU 1630 10.484 1.285 18.626 1.00 29.81 ATOM 1380 CD1 LEU 1630 9.119 1.983 18.745 1.00 28.46 ATOM 1381 CD2 LEU 1630 11.576 2.141 19.233 1.00 28.37 ATOM 1382 C LEU 1630 11.639 −2.242 19.904 1.00 29.32 ATOM 1383 O LEU 1630 11.414 −3.215 19.189 1.00 30.84 ATOM 1384 N VAL 1631 11.800 −2.342 21.221 1.00 28.90 ATOM 1386 CA VAL 1631 11.732 −3.629 21.905 1.00 26.84 ATOM 1387 CB VAL 1631 13.067 −3.919 22.670 1.00 28.88 ATOM 1388 CG1 VAL 1631 13.077 −5.341 23.236 1.00 21.54 ATOM 1389 CG2 VAL 1631 14.259 −3.699 21.744 1.00 24.30 ATOM 1390 C VAL 1631 10.561 −3.645 22.881 1.00 29.02 ATOM 1391 O VAL 1631 10.406 −2.737 23.706 1.00 29.31 ATOM 1392 N THR 1632 9.733 −4.674 22.764 1.00 30.84 ATOM 1394 CA THR 1632 8.562 −4.830 23.616 1.00 32.24 ATOM 1395 CB THR 1632 7.488 −5.685 22.912 1.00 31.45 ATOM 1396 OG1 THR 1632 7.896 −7.064 22.910 1.00 30.86 ATOM 1398 CG2 THR 1632 7.268 −5.194 21.470 1.00 28.04 ATOM 1399 C THR 1632 8.919 −5.493 24.943 1.00 34.17 ATOM 1400 O THR 1632 10.017 −6.019 25.105 1.00 35.02 ATOM 1401 N GLU 1633 7.959 −5.524 25.866 1.00 36.16 ATOM 1403 CA GLU 1633 8.155 −6.138 27.177 1.00 36.34 ATOM 1404 CB GLU 1633 6.865 −6.063 27.996 1.00 37.07 ATOM 1405 CG GLU 1633 6.957 −6.649 29.414 1.00 44.57 ATOM 1406 CD GLU 1633 8.035 −6.000 30.301 1.00 49.38 ATOM 1407 OE1 GLU 1633 8.124 −4.753 30.352 1.00 51.03 ATOM 1408 0E2 GLU 1633 8.788 −6.750 30.968 1.00 51.63 ATOM 1409 C GLU 1633 8.600 −7.585 27.042 1.00 36.42 ATOM 1410 O GLU 1633 9.347 −8.085 27.874 1.00 38.56 ATOM 1411 N ASP 1634 8.185 −8.240 25.964 1.00 37.70 ATOM 1413 CA ASP 1634 8.550 −9.637 25.737 1.00 38.53 ATOM 1414 CB ASP 1634 7.408 −10.378 25.027 1.00 44.08 ATOM 1415 CG ASP 1634 6.041 −10.106 25.657 1.00 51.60 ATOM 1416 OD1 ASP 1634 5.865 −10.367 26.867 1.00 52.37 ATOM 1417 0D2 ASP 1634 5.137 −9.631 24.933 1.00 57.23 ATOM 1418 C ASP 1634 9.826 −9.776 24.905 1.00 36.56 ATOM 1419 O ASP 1634 20.127 −10.865 24.430 1.00 36.74 ATOM 1420 N ASN 1635 10.569 −8.683 24.739 1.00 36.56 ATOM 1422 CA ASN 1635 11.819 −8.662 23.945 1.00 37.10 ATOM 1423 CB ASN 1635 12.888 −9.587 24.548 1.00 36.92 ATOM 1424 CG ASN 1635 13.226 −9.226 25.978 1.00 36.54 ATOM 1425 OD1 ASN 1635 13.275 −8.058 26.340 1.00 38.84 ATOM 1426 ND2 ASN 1635 13.423 −10.235 26.606 1.00 39.58 ATOM 1429 C ASN 1635 11.632 −8.980 22.451 1.00 34.78 ATOM 1430 O ASN 1635 12.446 −9.677 21.834 1.00 34.00 ATOM 1431 N VAL 1636 10.533 −8.498 21.880 1.00 31.35 ATOM 1433 CA VAL 1636 10.279 −8.711 20.469 1.00 29.76 ATOM 1434 CB VAL 1636 8.778 −8.946 20.181 1.00 30.60 ATOM 1435 CG1 VAL 1636 8.538 −9.081 18.675 1.00 30.38 ATOM 1436 CG2 VAL 1636 8.315 −10.209 20.897 1.00 28.51 ATOM 1437 C VAL 1636 10.768 −7.449 19.781 1.00 28.02 ATOM 1438 O VAL 1636 10.506 −6.351 20.254 1.00 25.87 ATOM 1439 N MET 1637 11.575 −7.624 18.738 1.00 28.15 ATOM 1441 CA MET 1637 12.119 −6.508 17.980 1.00 26.01 ATOM 1442 CB MET 1637 13.366 −6.953 17.204 1.00 27.82 ATOM 1443 CG MET 1637 14.479 −7.554 18.051 1.00 29.73 ATOM 1444 SD MET 1637 15.124 −6.410 19.288 1.00 29.96 ATOM 1445 CE MET 1637 15.120 −7.459 20.689 1.00 27.19 ATOM 1446 C MET 1637 11.040 −6.087 16.993 1.00 24.77 ATOM 1447 O MET 1637 10.480 −6.929 16.303 1.00 24.50 ATOM 1448 N LYS 1638 10.755 −4.791 16.931 1.00 25.74 ATOM 1450 CA LYS 1638 9.746 −4.258 16.029 1.00 23.67 ATOM 1451 CB LYS 1638 8.486 −3.888 16.799 1.00 21.78 ATOM 1452 CG LYS 1638 7.715 −5.092 17.298 1.00 24.60 ATOM 1453 CD LYS 1638 6.406 −4.683 18.005 1.00 23.87 ATOM 1454 CE LYS 1638 5.486 −5.897 18.256 1.00 23.06 ATOM 1455 NZ LYS 1638 4.871 −6.398 16.976 1.00 24.60 ATOM 1459 C LYS 1638 10.260 −3.042 15.293 1.00 24.37 ATOM 1460 O LYS 1638 10.658 −2.055 15.901 1.00 26.58 ATOM 1461 N ILE 1639 10.271 −3.119 13.971 1.00 25.69 ATOM 1463 CA ILE 1639 10.721 −2.005 13.148 1.00 25.94 ATOM 1464 CB TLE 1639 10.935 −2.447 11.668 1.00 26.49 ATOM 1465 CG2 ILE 1639 11.218 −1.236 10.762 1.00 21.19 ATOM 1466 CG1 ILE 1639 12.103 −3.433 11.604 1.00 27.58 ATOM 1467 CD1 ILE 1639 12.120 −4.232 10.355 1.00 32.96 ATOM 1468 C ILE 1639 9.675 −0.892 13.242 1.00 27.32 ATOM 1469 O ILE 1639 8.466 −1.133 13.103 1.00 25.45 ATOM 1470 N ALA 1640 10.156 0.320 13.498 1.00 27.43 ATOM 1472 CA ALA 1640 9.321 1.499 13.632 1.00 26.96 ATOM 1473 CB ALA 1640 9.557 2.133 15.006 1.00 25.21 ATOM 1474 C ALA 1640 9.641 2.510 12.538 1.00 26.80 ATOM 1475 O ALA 1640 10.691 2.446 11.896 1.00 27.55 ATOM 1476 N ASP 1641 8.716 3.440 12.328 1.00 27.06 ATOM 1478 CA ASP 1641 8.862 4.526 11.349 1.00 30.54 ATOM 1479 CB ASP 1641 9.993 5.484 11.753 1.00 33.12 ATOM 1480 CG ASP 1641 9.668 6.310 12.999 1.00 36.17 ATOM 1481 OD1 ASP 1641 10.477 7.203 13.334 1.00 42.24 ATOM 1482 OD2 ASP 1641 8.633 6.076 13.648 1.00 33.22 ATOM 1483 C ASP 1641 9.049 4.107 9.898 1.00 29.94 ATOM 1484 O ASP 1641 9.598 4.861 9.102 1.00 30.13 ATOM 1485 N PHE 1642 8.569 2.920 9.553 1.00 30.22 ATOM 1487 CA PHE 1642 8.680 2.426 8.191 1.00 30.91 ATOM 1488 CB PHE 1642 8.462 0.909 8.159 1.00 26.24 ATOM 1489 CG PHE 1642 7.156 0.470 8.750 1.00 27.82 ATOM 1490 CD1 PHE 1642 5.986 0.495 7.988 1.00 27.08 ATOM 1491 CD2 PHE 1642 7.089 0.026 10.066 1.00 26.70 ATOM 1492 CE1 PHE 1642 4.761 0.088 8.532 1.00 25.18 ATOM 1493 CE2 PHE 1642 5.872 −0.383 10.624 1.00 27.59 ATOM 1494 CZ PHE 1642 4.705 −0.354 9.855 1.00 28.05 ATOM 1495 C PHE 1642 7.729 3.139 7.219 1.00 33.35 ATOM 1496 O PHE 1642 7.983 3.165 6.018 1.00 36.19 ATOM 1497 N GLY 1643 6.661 3.746 7.736 1.00 32.76 ATOM 1499 CA GLY 1643 5.710 4.419 6.863 1.00 31.44 ATOM 1500 C GLY 1643 5.805 5.927 6.910 1.00 32.94 ATOM 1501 O GLY 1643 4.945 6.636 6.399 1.00 33.10 ATOM 1502 N LEU 1644 6.872 6.407 7.525 1.00 35.45 ATOM 1504 CA LEU 1644 7.124 7.828 7.684 1.00 39.04 ATOM 1505 CB LEU 1644 8.387 8.011 8.514 1.00 37.80 ATOM 1506 CG LEU 1644 8.414 9.120 9.549 1.00 42.51 ATOM 1507 CD1 LEU 1644 7.301 8.887 10.563 1.00 44.08 ATOM 1508 CD2 LEU 1644 9.779 9.127 10.243 1.00 44.47 ATOM 1509 C LEU 1644 7.259 8.580 6.357 1.00 42.20 ATOM 1510 O LEU 1644 7.895 8.107 5.414 1.00 44.14 ATOM 1511 N ALA 1645 6.607 9.732 6.267 1.00 43.89 ATOM 1513 CA ALA 1645 6.677 10.569 5.082 1.00 45.62 ATOM 1514 CB ALA 1645 5.463 11.493 5.028 1.00 45.06 ATOM 1515 C ALA 1645 7.966 11.388 5.186 1.00 45.82 ATOM 1516 O ALA 1645 8.240 11.994 6.228 1.00 45.85 ATOM 1517 N ARG 1646 8.766 11.389 4.129 1.00 45.16 ATOM 1519 CA ARG 1646 10.015 12.140 4.138 1.00 47.06 ATOM 1520 CB ARG 1646 11.126 11.318 4.794 1.00 48.00 ATOM 1521 C ARG 1646 10.445 12.546 2.742 1.00 46.83 ATOM 1522 O ARG 1646 10.429 11.729 1.823 1.00 45.76 ATOM 1523 N ASP 1647 10.807 13.814 2.578 1.00 48.96 ATOM 1525 CA ASP 1647 11.278 14.291 1.288 1.00 50.93 ATOM 1526 CB ASP 1647 10.938 15.769 1.073 1.00 52.33 ATOM 1527 CG ASP 1647 11.191 16.228 −0.360 1.00 55.93 ATOM 1528 OD1 ASP 1647 12.231 15.850 −0.956 1.00 52.58 ATOM 1529 OD2 ASP 1647 10.340 16.980 −0.896 1.00 59.54 ATOM 1530 C ASP 1647 12.789 14.104 1.336 1.00 50.78 ATOM 1531 O ASP 1647 13.491 14.803 2.077 1.00 48.32 ATOM 1532 N ILE 1648 13.274 13.144 0.556 1.00 50.84 ATOM 1534 CA ILE 1648 14.696 12.833 0.516 1.00 52.58 ATOM 1535 CB ILE 1648 14.984 11.571 −0.324 1.00 50.85 ATOM 1536 CG2 ILE 1648 14.204 10.386 0.241 1.00 49.34 ATOM 1537 CG1 ILE 1648 14.638 11.813 −1.801 1.00 48.22 ATOM 1538 CD1 ILE 1648 15.233 10.806 −2.754 1.00 42.86 ATOM 1539 C ILE 1648 15.523 13.999 −0.018 1.00 55.57 ATOM 1540 O ILE 1648 16.648 14.222 0.423 1.00 57.24 ATOM 1541 N HIS 1649 14.944 14.766 −0.936 1.00 56.80 ATOM 1543 CA HIS 1649 15.650 15.895 −1.520 1.00 58.03 ATOM 1544 CB HIS 1649 15.013 16.302 −2.859 1.00 8.71 ATOM 1545 CG HIS 1649 15.221 15.308 −3.958 1.00 60.28 ATOM 1546 CD2 HIS 1649 16.303 14.566 −4.306 1.00 60.74 ATOM 1547 ND1 HIS 1649 14.243 14.986 −4.874 1.00 61.70 ATOM 1549 CE1 HIS 1649 14.708 14.104 −5.742 1.00 61.86 ATOM 1550 NE2 HIS 1649 15.959 13.833 −5.417 1.00 60.98 ATOM 1552 C HIS 1649 15.721 17.093 −0.591 1.00 58.49 ATOM 1553 O HIS 1649 16.129 28.175 −1.004 1.00 60.56 ATOM 1554 N HIS 1650 15.285 16.916 0.654 1.00 59.58 ATOM 1556 CA HIS 1650 15.306 18.001 1.635 1.00 61.38 ATOM 1557 CB HIS 1650 13.898 18.540 1.863 1.00 65.28 ATOM 1558 CG HIS 1650 13.404 19.433 0.738 1.00 72.62 ATOM 1559 CD2 HIS 1650 13.492 20.752 0.536 1.00 76.23 ATOM 1560 ND1 HIS 1650 12.710 18.904 −0.339 1.00 77.05 ATOM 1562 CE1 HIS 1650 12.402 19.907 −1.157 1.00 78.51 ATOM 1563 NE2 HIS 1650 12.863 21.015 −0.647 1.00 78.82 ATOM 1565 C HIS 1650 15.925 17.575 2.972 1.00 60.63 ATOM 1566 O HIS 1650 15.796 18.271 3.969 1.00 60.20 ATOM 1567 N ILE 1651 16.584 16.419 2.987 1.00 60.22 ATOM 1569 CA ILE 1651 17.197 15.920 4.204 1.00 60.03 ATOM 1570 CB ILE 1651 17.574 14.434 4.069 1.00 62.54 ATOM 1571 CG2 ILE 1651 18.280 13.920 5.323 1.00 63.48 ATOM 1572 CG1 ILE 1651 16.329 13.584 3.800 1.00 65.18 ATOM 1573 CD1 ILE 1651 16.635 12.124 3.603 1.00 67.18 ATOM 1574 C ILE 1651 18.457 16.698 4.557 1.00 59.16 ATOM 1575 O ILE 1651 19.326 16.907 3.716 1.00 59.25 ATOM 1576 N ASP 1652 18.532 17.176 5.793 1.00 58.91 ATOM 1578 CA ASP 1652 19.702 17.915 6.260 1.00 58.25 ATOM 1579 CB ASP 1652 19.312 18.788 7.444 1.00 61.14 ATOM 1580 CG ASP 1652 20.506 19.569 8.028 1.00 65.33 ATOM 1581 OD1 ASP 1652 21.614 19.574 7.411 1.00 67.11 ATOM 1582 OD2 ASP 1652 20.337 20.191 9.126 1.00 69.04 ATOM 1583 C ASP 1652 20.786 16.922 6.676 1.00 56.75 ATOM 1584 O ASP 1652 20.699 16.307 7.741 1.00 56.06 ATOM 1585 N TYR 1653 21.794 16.762 5.826 1.00 55.40 ATOM 1587 CA TYR 1653 22.900 15.849 6.088 1.00 54.50 ATOM 1588 CB TYR 1653 23.825 15.783 4.872 1.00 52.80 ATOM 1589 CG TYR 1653 23.334 14.854 3.796 1.00 52.10 ATOM 1590 CD1 TYR 1653 24.123 14.566 2.685 1.00 51.50 ATOM 1591 CE1 TYR 1653 23.701 13.658 1.724 1.00 53.52 ATOM 1592 CD2 TYR 1653 22.099 14.214 3.917 1.00 52.88 ATOM 1593 CE2 TYR 1653 21.664 13.302 2.966 1.00 54.63 ATOM 1594 CZ TYR 1653 22.469 13.025 1.870 1.00 54.35 ATOM 1595 OH TYR 1653 22.049 12.107 0.933 1.00 53.23 ATOM 1597 C TYR 1653 23.717 16.158 7.339 1.00 55.40 ATOM 1598 O TYR 1653 24.381 15.284 7.900 1.00 54.47 ATOM 1599 N TYR 1654 23.673 17.409 7.773 1.00 56.72 ATOM 1601 CA TYR 1654 24.421 17.826 8.947 1.00 58.87 ATOM 1602 CB TYR 1654 24.978 19.235 8.733 1.00 57.91 ATOM 1603 CG TYR 1654 26.068 19.269 7.685 1.00 60.49 ATOM 1604 CD1 TYR 1654 25.760 19.301 6.325 1.00 61.37 ATOM 1605 CE1 TYR 1654 26.769 19.289 5.356 1.00 63.72 ATOM 1606 CD2 TYR 1654 27.412 19.227 8.053 1.00 61.74 ATOM 1607 CE2 TYR 1654 28.425 19.216 7.099 1.00 64.08 ATOM 1608 CZ TYR 1654 28.102 19.248 5.753 1.00 65.12 ATOM 1609 OH TYR 1654 29.117 19.248 4.817 1.00 64.17 ATOM 1611 C TYR 1654 23.628 17.732 10.245 1.00 60.17 ATOM 1612 O TYR 1654 24.173 17.935 11.335 1.00 61.09 ATOM 1613 N LYS 1655 22.348 17.393 10.133 1.00 60.54 ATOM 1615 CA LYS 1655 21.493 17.277 11.306 1.00 62.12 ATOM 1616 CB LYS 1655 20.019 17.382 10.910 1.00 64.32 ATOM 1617 CG LYS 1655 19.054 17.346 12.079 1.00 67.17 ATOM 1618 CD LYS 1655 17.644 17.608 11.602 1.00 73.05 ATOM 1619 CE LYS 1655 16.626 17.243 12.660 1.00 77.36 ATOM 1620 NZ LYS 1655 15.230 17.494 12.186 1.00 81.10 ATOM 1624 C LYS 1655 21.754 15.976 12.057 1.00 62.19 ATOM 1625 O LYS 1655 21.902 14.907 11.454 1.00 61.36 ATOM 1626 N LYS 1656 21.822 16.084 13.380 1.00 62.26 ATOM 1628 CA LYS 1656 22.069 14.933 14.236 1.00 62.28 ATOM 1629 CB LYS 1656 23.027 15.310 15.372 1.00 62.05 ATOM 1630 CG LYS 1656 24.474 15.489 14.957 1.00 62.62 ATOM 1631 CD LYS 1656 25.320 15.889 16.157 1.00 66.45 ATOM 1632 CE LYS 1656 26.803 15.666 15.908 1.00 67.28 ATOM 1633 NZ LYS 1656 27.619 16.007 17.109 1.00 68.45 ATOM 1637 C LYS 1656 20.774 14.381 14.824 1.00 61.86 ATOM 1638 O LYS 1656 19.714 15.007 14.733 1.00 62.95 ATOM 1639 N THR 1657 20.875 13.198 15.420 1.00 60.10 ATOM 1641 CA THR 1657 19.743 12.541 16.053 1.00 57.73 ATOM 1642 CB THR 1657 19.973 11.012 16.121 1.00 56.04 ATOM 1643 OG1 THR 1657 21.150 10.730 16.896 1.00 55.21 ATOM 1645 CG2 THR 1657 20.152 10.431 14.731 1.00 53.07 ATOM 1646 C THR 1657 19.664 13.102 17.472 1.00 57.74 ATOM 1647 O THR 1657 20.513 13.899 17.870 1.00 57.76 ATOM 1648 N THR 1658 18.678 12.667 18.249 1.00 58.80 ATOM 1650 CA THR 1658 18.548 13.140 19.627 1.00 60.33 ATOM 1651 CB THR 1658 17.318 12.517 20.290 1.00 61.37 ATOM 1652 C THR 1658 19.811 42.779 20.406 1.00 60.43 ATOM 1653 O THR 1658 20.350 13.599 21.155 1.00 60.59 ATOM 1654 N ASN 1659 20.311 11.567 20.161 1.00 59.97 ATOM 1656 CA ASN 1659 21.508 11.058 20.827 1.00 58.28 ATOM 1657 CB ASN 1659 21.607 9.545 20.645 1.00 59.95 ATOM 1658 CG ASN 1659 22.444 8.883 21.723 1.00 60.10 ATOM 1659 OD1 ASN 1659 22.382 9.265 22.891 1.00 61.26 ATOM 1660 ND2 ASN 1659 23.210 7.867 21.341 1.00 57.09 ATOM 1663 C ASN 1659 22.781 11.717 20.311 1.00 57.13 ATOM 1664 O ASN 1659 23.868 11.418 20.793 1.00 57.34 ATOM 1665 N GLY 1660 22.643 12.570 19.299 1.00 56.48 ATOM 1667 CA GLY 1660 23.781 13.276 18.733 1.00 54.87 ATOM 1668 C GLY 1660 24.539 12.570 17.623 1.00 53.04 ATOM 1669 O GLY 1660 25.716 12.855 17.394 1.00 54.11 ATOM 1670 N ARG 1661 23.879 11.659 16.918 1.00 51.37 ATOM 1672 CA ARG 1661 24.536 10.930 15.833 1.00 48.96 ATOM 1673 CB ARG 1661 24.283 9.428 15.961 1.00 48.48 ATOM 1674 CG ARG 1661 24.848 8.796 17.215 1.00 50.03 ATOM 1675 CD ARG 1661 24.492 7.325 17.234 1.00 50.78 ATOM 1676 NE ARG 1661 25.013 6.614 18.396 1.00 50.11 ATOM 1678 CZ ARG 1661 24.902 5.299 18.566 1.00 50.08 ATOM 1679 NH1 ARG 1661 24.286 4.560 17.645 1.00 46.57 ATOM 1682 NH2 ARG 1661 25.426 4.717 19.643 1.00 47.88 ATOM 1685 C ARG 1661 24.076 11.422 14.459 1.00 46.53 ATOM 1686 O ARG 1661 23.031 12.029 14.325 1.00 45.01 ATOM 1687 N LEU 1662 24.839 11.094 13.432 1.00 42.39 ATOM 1689 CA LEU 1662 24.546 11.503 12.076 1.00 40.71 ATOM 1690 CB LEU 1662 25.823 12.031 11.399 1.00 40.25 ATOM 1691 CG LEU 1662 26.408 13.332 11.965 1.00 42.44 ATOM 1692 CD1 LEU 1662 27.853 13.478 11.537 1.00 40.42 ATOM 1693 CD2 LEU 1662 25.591 14.536 11.514 1.00 41.16 ATOM 1694 C LEU 1662 23.946 10.362 11.258 1.00 38.45 ATOM 1695 O LEU 1662 24.647 9.436 10.862 1.00 36.67 ATOM 1696 N PRO 1663 22.632 10.428 10.987 1.00 37.09 ATOM 1697 CD PRO 1663 21.717 11.475 11.489 1.00 38.18 ATOM 1698 CA PRO 1663 21.894 9.424 10.207 1.00 35.59 ATOM 1699 CB PRO 1663 20.535 10.098 9.983 1.00 35.90 ATOM 1700 CG PRO 1663 20.343 10.856 11.258 1.00 39.13 ATOM 1701 C PRO 1663 22.556 9.045 8.876 1.00 33.05 ATOM 1702 O PRO 1663 22.362 7.933 8.378 1.00 31.16 ATOM 1703 N VAL 1664 23.333 9.960 8.299 1.00 32.07 ATOM 1705 CA VAL 1664 24.020 9.669 7.034 1.00 32.49 ATOM 1706 CB VAL 1664 24.831 10.886 6.477 1.00 32.68 ATOM 1707 CG1 VAL 1664 23.898 11.906 5.864 1.00 32.25 ATOM 1708 CG2 VAL 1664 25.670 11.523 7.571 1.00 33.22 ATOM 1709 C VAL 1664 24.957 8.469 7.171 1.00 29.57 ATOM 1710 O VAL 1664 25.328 7.864 6.175 1.00 27.39 ATOM 1711 N LYS 1665 25.303 8.116 8.409 1.00 28.82 ATOM 1713 CA LYS 1665 26.189 6.991 8.673 1.00 27.87 ATOM 1714 CB LYS 1665 26.815 7.100 10.065 1.00 26.99 ATOM 1715 CG LYS 1665 27.967 8.089 10.079 1.00 29.23 ATOM 1716 CD LYS 1665 28.283 8.619 11.466 1.00 30.64 ATOM 1717 CE LYS 1665 29.543 9.478 11.426 1.00 30.94 ATOM 1718 NZ LYS 1665 29.826 10.128 12.737 1.00 31.63 ATOM 1722 C LYS 1665 25.546 5.637 8.465 1.00 26.76 ATOM 1723 O LYS 1665 26.211 4.615 8.589 1.00 26.78 ATOM 1724 N TRP 1666 24.260 5.630 8.137 1.00 25.79 ATOM 1726 CA TRP 1666 23.561 4.381 7.865 1.00 26.56 ATOM 1727 CB TRP 1666 22.299 4.273 8.724 1.00 25.63 ATOM 1728 CG TRP 1666 22.564 3.872 10.174 1.00 26.95 ATOM 1729 CD2 TRP 1666 23.052 4.717 11.232 1.00 24.83 ATOM 1730 CE2 TRP 1666 23.134 3.920 12.398 1.00 24.49 ATOM 1731 CE3 TRP 1666 23.433 6.062 11.306 1.00 24.54 ATOM 1732 CD1 TRP 1666 22.376 2.636 10.730 1.00 20.10 ATOM 1733 NE1 TRP 1666 22.716 2.660 12.063 1.00 21.86 ATOM 1735 CZ2 TRP 1666 23.575 4.433 13.627 1.00 25.71 ATOM 1736 CZ3 TRP 1666 23.870 6.569 12.523 1.00 26.00 ATOM 1737 CH2 TRP 1666 23.939 5.754 13.665 1.00 26.04 ATOM 1738 C TRP 1666 23.188 4.263 6.386 1.00 23.62 ATOM 1739 O TRP 1666 22.754 3.214 5.931 1.00 24.87 ATOM 1740 N MET 1667 23.404 5.330 5.631 1.00 22.78 ATOM 1742 CA MET 1667 23.046 5.361 4.215 1.00 23.73 ATOM 1743 CB MET 1667 22.894 6.802 3.744 1.00 26.24 ATOM 1744 CG MET 1667 21.823 7.621 4.434 1.00 35.55 ATOM 1745 SD MET 1667 21.795 9.276 3.706 1.00 42.23 ATOM 1746 CE MET 1667 21.019 8.904 2.238 1.00 40.57 ATOM 1747 C MET 1667 23.991 4.693 3.239 1.00 22.77 ATOM 1748 O MET 1667 25.205 4.894 3.294 1.00 24.25 ATOM 1749 N ALA 1668 23.420 3.963 2.286 1.00 22.73 ATOM 1751 CA ALA 1668 24.217 3.337 1.237 1.00 23.54 ATOM 1752 CB ALA 1668 23.339 2.495 0.340 1.00 21.80 ATOM 1753 C ALA 1668 24.805 4.495 0.430 1.00 25.53 ATOM 1754 O ALA 1668 24.181 5.551 0.316 1.00 23.66 ATOM 1755 N PRO 1669 26.006 4.314 −0.153 1.00 26.86 ATOM 1756 CD PRO 1669 26.899 3.144 −0.095 1.00 26.35 ATOM 1757 CA PRO 1669 26.611 5.390 −0.942 1.00 27.78 ATOM 1758 CB PRO 1669 27.864 4.731 −1.518 1.00 25.51 ATOM 1759 CG PRO 1669 28.225 3.741 −0.471 1.00 25.36 ATOM 1760 C PRO 1669 25.686 5.900 −2.057 1.00 26.47 ATOM 1761 O PRO 1669 25.617 7.099 −2.288 1.00 28.42 ATOM 1762 N GLU 1670 24.951 5.010 −2.724 1.00 26.88 ATOM 1764 CA GLU 1670 24.057 5.459 −3.796 1.00 29.03 ATOM 1765 CB GLU 1670 23.597 4.293 −4.693 1.00 31.79 ATOM 1766 CG GLU 1670 22.588 3.325 −4.065 1.00 32.47 ATOM 1767 CD GLU 1670 23.212 2.184 −3.255 1.00 32.43 ATOM 1768 OE1 GLU 1670 22.429 1.297 −2.822 1.00 25.01 ATOM 1769 OE2 GLU 1670 24.458 2.157 −3.069 1.00 28.75 ATOM 1770 C GLU 1670 22.864 6.274 −3.294 1.00 28.37 ATOM 1771 O GLU 1670 22.358 7.146 −4.001 1.00 25.72 ATOM 1772 N ALA 1671 22.451 6.028 −2.053 1.00 30.08 ATOM 1774 CA ALA 1671 21.347 6.779 −1.465 1.00 31.24 ATOM 1775 CB ALA 1671 20.751 6.031 −0.287 1.00 26.42 ATOM 1776 C ALA 1671 21.899 8.125 −1.013 1.00 31.36 ATOM 1777 O ALA 1671 21.298 9.167 −1.249 1.00 33.11 ATOM 1778 N LEU 1672 23.068 8.096 −0.387 1.00 32.73 ATOM 1780 CA LEU 1672 23.715 9.304 0.100 1.00 33.96 ATOM 1781 CB LEU 1672 24.931 8.935 0.940 1.00 33.89 ATOM 1782 CG LEU 1672 25.783 10.071 1.502 1.00 37.62 ATOM 1783 CD1 LEU 1672 25.010 10.800 2.581 1.00 39.57 ATOM 1784 CD2 LEU 1672 27.054 9.491 2.087 1.00 32.30 ATOM 1785 C LEU 1672 24.157 10.207 −1.042 1.00 36.83 ATOM 1786 O LEU 1672 23.769 11.369 −1.102 1.00 37.87 ATOM 1787 N PHE 1673 24.959 9.669 −1.954 1.00 35.82 ATOM 1789 CA PHE 1673 25.466 10.449 −3.071 1.00 35.82 ATOM 1790 CB PHE 1673 26.738 9.802 −3.639 1.00 34.66 ATOM 1791 CG PHE 1673 27.850 9.642 −2.634 1.00 33.84 ATOM 1792 CD1 PHE 1673 28.503 8.422 −2.494 1.00 32.65 ATOM 1793 CD2 PHE 1673 28.242 10.709 −1.827 1.00 36.98 ATOM 1794 CE1 PHE 1673 29.540 8.257 −1.555 1.00 37.95 ATOM 1795 CE2 PHE 1673 29.279 10.557 −0.881 1.00 39.90 ATOM 1796 CZ PHE 1673 29.927 9.325 −0.748 1.00 37.09 ATOM 1797 C PHE 1673 24.483 10.692 −4.210 1.00 36.34 ATOM 2798 O PHE 1673 24.430 11.788 −4.754 1.00 37.18 ATOM 1799 N ASP 1674 23.705 9.677 −4.568 1.00 38.22 ATOM 1801 CA ASP 1674 22.780 9.777 −5.693 1.00 38.51 ATOM 1802 CB ASP 1674 23.008 8.597 −6.633 1.00 40.34 ATOM 1803 CG ASP 1674 24.439 8.511 −7.122 1.00 43.87 ATOM 1804 OD1 ASP 1674 25.092 9.571 −7.254 1.00 42.79 ATOM 1805 OD2 ASP 1674 24.906 7.376 −7.369 1.00 47.94 ATOM 1806 C ASP 1674 21.298 9.853 −5.360 1.00 40.21 ATOM 1807 O ASP 1674 20.457 9.872 −6.271 1.00 39.07 ATOM 1808 N ARG 1675 20.975 9.836 −4.072 1.00 39.83 ATOM 1810 CA ARG 1675 19.589 9.900 −3.631 1.00 42.25 ATOM 1811 CB ARG 1675 18.992 11.271 −3.964 1.00 48.19 ATOM 1812 CG ARG 1675 19.691 12.420 −3.267 1.00 59.20 ATOM 1813 CD ARG 1675 19.462 13.729 −4.019 1.00 67.81 ATOM 1814 NE ARG 1675 20.079 14.876 −3.352 1.00 75.11 ATOM 1816 CZ ARG 1675 19.688 16.136 −3.525 1.00 78.74 ATOM 1817 NH1 ARG 1675 18.680 16.429 −4.341 1.00 79.91 ATOM 1820 NH2 ARG 1675 20.311 17.115 −2.890 1.00 81.24 ATOM 1823 C ARG 1675 18.730 8.777 −4.221 1.00 39.00 ATOM 1824 O ARG 1675 17.544 8.956 −4.488 1.00 39.71 ATOM 1825 N ILE 1676 19.345 7.624 −4.434 1.00 35.50 ATOM 1827 CA ILE 1676 18.636 6.471 −4.958 1.00 33.51 ATOM 1828 CB ILE 1676 19.434 5.759 −6.039 1.00 34.59 ATOM 1829 CG2 ILE 1676 18.582 4.678 −6.649 1.00 33.90 ATOM 1830 CG1 ILE 1676 19.848 6.752 −7.120 1.00 37.60 ATOM 1831 CD1 ILE 1676 20.861 6.197 −8.109 1.00 42.67 ATOM 1832 C ILE 1676 18.390 5.501 −3.809 1.00 30.94 ATOM 1833 O ILE 1676 19.326 4.926 −3.252 1.00 28.62 ATOM 1834 N TYR 1677 17.124 5.351 −3.443 1.00 30.60 ATOM 1836 CA TYR 1677 16.724 4.467 −2.359 1.00 25.87 ATOM 1837 CB TYR 1677 15.781 5.197 −1.413 1.00 26.40 ATOM 1838 CG TYR 1677 16.483 6.220 −0.555 1.00 27.67 ATOM 1839 CD1 TYR 1677 16.663 7.533 −0.999 1.00 27.45 ATOM 1840 CE1 TYR 1677 17.269 8.483 −0.191 1.00 26.55 ATOM 1841 CD2 TYR 1677 16.935 5.883 0.721 1.00 24.58 ATOM 1842 CE2 TYR 1677 17.536 6.828 1.538 1.00 26.35 ATOM 1843 CZ TYR 1677 17.698 8.122 1.080 1.00 28.80 ATOM 1844 OH TYR 1677 18.270 9.059 1.914 1.00 34.97 ATOM 1846 C TYR 1677 16.055 3.235 −2.911 1.00 22.70 ATOM 1847 O TYR 1677 15.144 3.335 −3.728 1.00 26.22 ATOM 1848 N THR 1678 16.477 2.076 −2.420 1.00 21.83 ATOM 1850 CA THR 1678 15.968 0.791 −2.865 1.00 22.14 ATOM 1851 CB THR 1678 16.907 0.191 −3.928 1.00 23.91 ATOM 1852 OG1 THR 1678 18.229 0.105 −3.373 1.00 27.47 ATOM 1854 CG2 THR 1678 16.949 1.053 −5.188 1.00 24.94 ATOM 1855 C THR 1678 15.999 −0.176 −1.692 1.00 22.79 ATOM 1856 O THR 1678 16.427 0.170 −0.592 1.00 23.39 ATOM 1857 N HIS 1679 15.563 −1.402 −1.929 1.00 21.98 ATOM 1859 CA HIS 1679 15.613 −2.417 −0.888 1.00 22.97 ATOM 1860 CB HIS 1679 14.872 −3.671 −1.351 1.00 22.04 ATOM 1861 CG HIS 1679 13.421 −3.444 −1.621 1.00 25.41 ATOM 1862 CD2 HIS 1679 12.674 −3.611 −2.740 1.00 26.60 ATOM 1863 ND1 HIS 1679 12.556 −2.954 −0.663 1.00 26.13 ATOM 1865 CE1 HIS 1679 11.348 −2.830 −1.178 1.00 28.66 ATOM 1866 NE2 HIS 1679 11.394 −3.221 −2.441 1.00 29.66 ATOM 1868 C HIS 1679 37.097 −2.719 −0.650 1.00 23.14 ATOM 1869 O HIS 1679 17.511 −3.074 0.459 1.00 21.69 ATOM 1870 N GLN 1680 17.895 −2.506 −1.697 1.00 22.38 ATOM 1872 CA GLN 1680 19.335 −2.726 −1.658 1.00 22.33 ATOM 1873 CB GLN 1680 19.948 −2.594 −3.058 1.00 22.52 ATOM 1874 CG GLN 1680 19.895 −3.872 −3.879 1.00 29.15 ATOM 1875 CD GLN 1680 18.865 −3.847 −4.991 1.00 33.60 ATOM 1876 OE1 GLN 1680 17.819 −3.212 −4.871 1.00 38.43 ATOM 1879 NE2 GLN 1680 19.159 −4.542 −6.085 1.00 33.44 ATOM 1880 C GLN 1680 20.007 −1.740 −0.732 1.00 22.61 ATOM 1881 O GLN 1680 20.943 −2.093 −0.027 1.00 22.00 ATOM 1882 N SER 1681 19.562 −0.490 −0.745 1.00 22.06 ATOM 1884 CA SER 1681 20.184 0.479 0.137 1.00 23.41 ATOM 1885 CB SER 1681 19.886 1.923 −0.306 1.00 20.06 ATOM 1886 OG SER 1681 18.503 2.166 −0.479 1.00 22.90 ATOM 1688 C SER 1681 19.778 0.206 1.583 1.00 23.08 ATOM 1889 O SER 1681 20.528 0.531 2.506 1.00 24.13 ATOM 1890 N ASP 1682 18.608 −0.412 1.770 1.00 23.19 ATOM 1892 CA ASP 1682 18.107 −0.775 3.104 1.00 22.37 ATOM 1893 CB ASP 1682 16.660 −1.275 3.018 1.00 24.55 ATOM 1894 CG ASP 1682 15.626 −0.172 3.222 1.00 24.22 ATOM 1895 OD1 ASP 1682 14.428 −0.479 3.005 1.00 25.02 ATOM 1896 OD2 ASP 1682 15.949 0.963 3.625 1.00 24.82 ATOM 1897 C ASP 1682 18.980 −1.888 3.690 1.00 20.47 ATOM 1898 O ASP 1682 19.172 −1.984 4.906 1.00 21.83 ATOM 1899 N VAL 1683 19.480 −2.746 2.806 1.00 20.14 ATOM 1901 CA VAL 1683 20.340 −3.856 3.179 1.00 20.49 ATOM 1902 CB VAL 1683 20.493 −4.842 2.003 1.00 22.38 ATOM 1903 CG1 VAL 1683 21.757 −5.691 2.159 1.00 19.57 ATOM 1904 CG2 VAL 1683 19.264 −5.740 1.942 1.00 22.35 ATOM 1905 C VAL 1683 21.677 −3.315 3.683 1.00 20.22 ATOM 1906 O VAL 1683 22.202 −3.789 4.684 1.00 21.41 ATOM 1907 N TRP 1684 22.210 −2.311 3.003 1.00 21.33 ATOM 1909 CA TRP 1684 23.440 −1.666 3.449 1.00 22.21 ATOM 1910 CB TRP 1684 23.768 −0.473 2.540 1.00 18.78 ATOM 1911 CG TRP 1684 24.924 0.391 3.037 1.00 22.80 ATOM 1912 CD2 TRP 1684 26.237 0.477 2.472 1.00 24.60 ATOM 1913 CE2 TRP 1684 26.989 1.364 3.286 1.00 24.34 ATOM 1914 CE3 TRP 1684 26.853 −0.099 1.352 1.00 24.32 ATOM 1915 CD1 TRP 1684 24.933 1.208 4.138 1.00 22.28 ATOM 1916 NE1 TRP 1684 26.169 1.792 4.297 1.00 22.32 ATOM 1918 CZ2 TRP 1684 28.324 1.669 3.022 1.00 24.77 ATOM 1919 CZ3 TRP 1684 28.193 0.213 1.090 1.00 24.46 ATOM 1920 CH2 TRP 1684 28.906 1.088 1.918 1.00 24.00 ATOM 1921 C TRP 1684 23.198 −1.183 4.899 1.00 23.26 ATOM 1922 O TRP 1684 23.982 −1.475 5.805 1.00 24.52 ATOM 1923 N SER 1685 22.108 −0.447 5.113 1.00 22.88 ATOM 1925 CA SER 1685 21.744 0.057 6.444 1.00 24.01 ATOM 1926 CB SER 1685 20.398 0.783 6.385 1.00 21.90 ATOM 1927 OG SER 1685 20.424 1.787 5.388 1.00 24.75 ATOM 1929 C SER 1685 21.659 −1.087 7.464 1.00 24.28 ATOM 1930 O SER 1685 22.077 −0.933 8.625 1.00 23.94 ATOM 1931 N PHE 1686 21.099 −2.221 7.037 1.00 23.20 ATOM 1933 CA PHE 1686 20.993 −3.393 7.898 1.00 23.87 ATOM 1934 CB PHE 1686 20.216 −4.519 7.216 1.00 19.56 ATOM 1935 CG PHE 1686 20.062 −5.734 8.075 1.00 22.19 ATOM 1936 CD1 PHE 1686 19.240 −5.701 9.203 1.00 21.55 ATOM 1937 CD2 PHE 1686 20.773 −6.899 7.793 1.00 21.94 ATOM 1938 CE1 PHE 1686 19.125 −6.801 10.033 1.00 21.66 ATOM 1939 CE2 PHE 1686 20.663 −8.012 8.623 1.00 22.47 ATOM 1940 CZ PHE 1686 19.842 −7.961 9.743 1.00 23.14 ATOM 1941 C PHE 1686 22.389 −3.890 8.300 1.00 22.62 ATOM 1942 O PHE 1686 22.579 −4.424 9.407 1.00 23.09 ATOM 1943 N GLY 1687 23.354 −3.726 7.401 1.00 23.50 ATOM 1945 CA GLY 1687 24.718 −4.110 7.721 1.00 23.83 ATOM 1946 C GLY 1687 25.230 −3.247 8.867 1.00 21.95 ATOM 1947 O GLY 1687 25.901 −3.749 9.778 1.00 23.76 ATOM 1948 N VAL 1688 24.928 −1.947 8.817 1.00 20.60 ATOM 1950 CA VAL 1688 25.331 −1.009 9.877 1.00 22.34 ATOM 1951 CB VAL 1688 25.020 0.481 9.488 1.00 20.94 ATOM 1952 CG1 VAL 1688 25.547 1.438 10.543 1.00 21.65 ATOM 1953 CG2 VAL 1688 25.675 0.832 8.160 1.00 22.71 ATOM 1954 C VAL 1688 24.598 −1.400 11.182 1.00 22.71 ATOM 1955 O VAL 1688 25.199 −1.479 12.255 1.00 22.78 ATOM 1956 N LEU 1689 23.310 −1.706 11.082 1.00 22.81 ATOM 1958 CA LEU 1689 22.534 −2.111 12.253 1.00 25.21 ATOM 1959 CB LEU 1689 21.064 −2.357 11.866 1.00 25.78 ATOM 1960 CG LEU 1689 20.006 −2.491 12.976 1.00 29.18 ATOM 1961 CD1 LEU 1689 18.643 −2.109 12.408 1.00 28.57 ATOM 1962 CD2 LEU 1689 19.959 −3.895 13.553 1.00 26.77 ATOM 1963 C LEU 1689 23.158 −3.375 12.871 1.00 25.88 ATOM 1964 O LEU 1689 23.249 −3.483 14.099 1.00 26.50 ATOM 1965 N LEU 1690 23.588 −4.323 12.031 1.00 25.84 ATOM 1967 CA LEU 1690 24.221 −5.544 12.523 1.00 24.43 ATOM 1968 CB LEU 1690 24.669 −6.444 11.377 1.00 26.35 ATOM 1969 CG LEU 1690 23.672 −7.309 10.604 1.00 26.57 ATOM 1970 CD1 LEU 1690 24.415 −7.962 9.446 1.00 26.33 ATOM 1971 CD2 LEU 1690 23.042 −8.380 11.502 1.00 24.66 ATOM 1972 C LEU 1690 25.430 −5.168 13.349 1.00 25.22 ATOM 1973 O LEU 1690 25.646 −5.706 14.435 1.00 24.84 ATOM 1974 N TRP 1691 26.211 −4.227 12.826 1.00 26.92 ATOM 1976 CA TRP 1691 27.405 −3.728 13.504 1.00 25.77 ATOM 1977 CB TRP 1691 28.072 −2.659 12.631 1.00 24.82 ATOM 1978 CG TRP 1691 29.394 −2.195 13.154 1.00 27.98 ATOM 1979 CD2 TRP 1691 29.623 −1.104 14.056 1.00 26.95 ATOM 1980 CE2 TRP 1691 31.022 −1.015 14.259 1.00 27.64 ATOM 1981 CE3 TRP 1691 28.783 −0.191 14.708 1.00 26.28 ATOM 1982 CD1 TRP 1691 30.634 −2.715 12.856 1.00 28.38 ATOM 1983 NE1 TRP 1691 31.609 −2.009 13.518 1.00 29.56 ATOM 1985 CZ2 TRP 1691 31.599 −0.045 15.086 1.00 27.78 ATOM 1986 CZ3 TRP 1691 29.356 0.769 15.533 1.00 27.63 ATOM 1987 CH2 TRP 1691 30.753 0.835 15.713 1.00 30.68 ATOM 1988 C TRP 1691 27.025 −3.147 14.876 1.00 26.38 ATOM 1989 O TRP 1691 27.686 −3.414 15.883 1.00 24.82 ATOM 1990 N GLU 1692 25.926 −2.393 14.916 1.00 27.62 ATOM 1992 CA GLU 1692 25.442 −1.790 16.162 1.00 27.02 ATOM 1993 CB GLU 1692 24.193 −0.963 15.919 1.00 29.27 ATOM 1994 OG GLU 1692 24.345 0.236 15.028 1.00 24.77 ATOM 1995 CD GLU 1692 23.046 0.992 14.962 1.00 25.98 ATOM 1996 OE1 GLU 1692 22.238 0.694 14.058 1.00 22.29 ATOM 1997 OE2 GLU 1692 22.803 1.837 15.850 1.00 25.12 ATOM 1998 C GLU 1692 25.092 −2.856 17.191 1.00 27.88 ATOM 1999 O GLU 1692 25.333 −2.673 18.379 1.00 30.18 ATOM 2000 N ILE 1693 24.500 −3.956 16.734 1.00 26.65 ATOM 2002 CA ILE 1693 24.118 −5.054 17.618 1.00 26.14 ATOM 2003 CB ILE 1693 23.279 −6.144 16.858 1.00 25.37 ATOM 2004 CG2 ILE 1693 23.144 −7.445 17.704 1.00 21.48 ATOM 2005 CG1 ILE 1693 21.897 −5.563 16.496 1.00 24.80 ATOM 2006 CD1 ILE 1693 21.017 −6.479 15.642 1.00 22.40 ATOM 2007 C ILE 1693 25.345 −5.698 18.239 1.00 27.17 ATOM 2008 O ILE 1693 25.424 −5.864 19.452 1.00 27.30 ATOM 2009 N PHE 1694 26.329 −6.017 17.414 1.00 29.98 ATOM 2011 CA PHE 1694 27.518 −6.674 17.925 1.00 30.61 ATOM 2012 CB PHE 1694 28.140 −7.556 16.843 1.00 28.30 ATOM 2013 CG PHE 1694 27.197 −8.611 16.353 1.00 30.91 ATOM 2014 CD1 PHE 1694 26.627 −8.526 15.088 1.00 34.46 ATOM 2015 CD2 PHE 1694 26.743 −9.601 17.224 1.00 32.71 ATOM 2016 CE1 PHE 1694 25.622 −9.409 14.701 1.00 34.24 ATOM 2017 CE2 PHE 1694 25.737 −10.490 16.844 1.00 32.44 ATOM 2018 CZ PHE 1694 25.170 −10.387 15.592 1.00 32.70 ATOM 2019 C PHE 1694 28.512 −5.796 18.689 1.00 31.74 ATOM 2020 O PHE 1694 29.469 −6.299 19.276 1.00 35.15 ATOM 2021 N THR 1695 28.275 −4.489 18.698 1.00 31.12 ATOM 2023 CA THR 1695 29.101 −3.575 19.473 1.00 29.96 ATOM 2024 CB THR 1695 29.532 −2.351 18.657 1.00 28.09 ATOM 2025 OG1 THR 1695 28.373 −1.685 18.150 1.00 30.65 ATOM 2027 CG2 THR 1695 30.450 −2.767 17.510 1.00 23.37 ATOM 2028 C THR 1695 28.240 −3.128 20.664 1.00 30.01 ATOM 2029 O THR 1695 28.617 −2.233 21.427 1.00 31.14 ATOM 2036 N LEU 1696 27.078 −3.766 20.797 1.00 27.96 ATOM 2032 CA LEU 1696 26.113 −3.490 21.862 1.00 30.25 ATOM 2033 CB LEU 1696 26.633 −3.985 23.216 1.00 33.54 ATOM 2034 CG LEU 1696 26.899 −5.482 23.339 1.00 32.61 ATOM 2035 CD1 LEU 1696 27.473 −5.777 24.711 1.00 33.54 ATOM 2036 CD2 LEU 1696 25.602 −6.233 23.126 1.00 36.37 ATOM 2037 C LEU 1696 25.717 −2.031 21.958 1.00 28.19 ATOM 2038 O LEU 1696 25.792 −1.431 23.018 1.00 29.18 ATOM 2039 N GLY 1697 25.251 −1.472 20.853 1.00 28.24 ATOM 2041 CA GLY 1697 24.851 −0.082 20.858 1.00 28.29 ATOM 2042 C GLY 1697 25.990 0.845 20.499 1.00 27.68 ATOM 2043 O GLY 1697 25.960 2.022 20.846 1.00 29.79 ATOM 2044 N GLY 1698 26.986 0.324 19.790 1.00 29.23 ATOM 2046 CA GLY 1698 28.115 1.143 19.396 1.00 30.79 ATOM 2047 C GLY 1698 27.743 2.212 18.388 1.00 32.38 ATOM 2048 O GLY 1698 26.817 2.044 17.601 1.00 33.26 ATOM 2049 N SER 1699 28.480 3.314 18.411 1.00 30.81 ATOM 2051 CA SER 1699 28.268 4.437 17.510 1.00 32.03 ATOM 2052 CB SER 1699 28.528 5.728 18.288 1.00 34.81 ATOM 2053 OG SER 1699 28.559 6.862 17.440 1.00 40.03 ATOM 2055 C SER 1699 29.198 4.325 16.282 1.00 32.20 ATOM 2056 O SER 1699 30.428 4.325 16.408 1.00 31.67 ATOM 2057 N PRO 1700 28.620 4.148 15.082 1.00 32.62 ATOM 2058 CD PRO 1700 27.178 4.142 14.773 1.00 34.19 ATOM 2059 CA PRO 1700 29.422 4.028 13.856 1.00 31.76 ATOM 2060 CB PRO 1700 28.357 3.830 12.759 1.00 32.04 ATOM 2061 CG PRO 1700 27.145 3.351 13.502 1.00 33.17 ATOM 2062 C PRO 1700 30.214 5.309 13.609 1.00 28.70 ATOM 2063 O PRO 1700 29.715 6.391 13.871 1.00 28.57 ATOM 2064 N TYR 1701 31.459 5.181 13.164 1.00 28.61 ATOM 2066 CA TYR 1701 32.311 6.338 12.870 1.00 29.92 ATOM 2067 CB TYR 1701 31.920 6.946 11.510 1.00 30.15 ATOM 2068 CG TYR 1701 31.965 5.994 10.339 1.00 36.17 ATOM 2069 CD1 TYR 1701 30.799 5.630 9.664 1.00 39.26 ATOM 2070 CE1 TYR 1701 30.839 4.767 8.571 1.00 41.51 ATOM 2071 CD2 TYR 1701 33.176 5.467 9.893 1.00 37.48 ATOM 2072 CE2 TYR 1701 33.229 4.607 8.805 1.00 42.94 ATOM 2073 CZ TYR 1701 32.059 4.263 8.146 1.00 45.72 ATOM 2074 OH TYR 1701 32.110 3.431 7.043 1.00 53.99 ATOM 2076 C TYR 1701 32.279 7.448 13.941 1.00 31.09 ATOM 2077 O TYR 1701 31.935 8.592 13.649 1.00 31.93 ATOM 2078 N PRO 1702 32.649 7.135 15.189 1.00 34.66 ATOM 2079 CD PRO 1702 33.212 5.879 15.708 1.00 36.83 ATOM 2080 CA PRO 1702 32.631 8.173 16.231 1.00 33.54 ATOM 2081 CB PRO 1702 33.116 7.432 17.479 1.00 32.18 ATOM 2082 CG PRO 1702 32.903 6.001 17.175 1.00 40.82 ATOM 2083 C PRO 1702 33.628 9.274 15.883 1.00 34.78 ATOM 2084 O PRO 1702 34.750 8.981 15.455 1.00 33.97 ATOM 2085 N GLY 1703 33.220 10.528 16.074 1.00 36.45 ATOM 2087 CA GLY 1703 34.085 11.667 15.788 1.00 34.40 ATOM 2088 C GLY 1703 34.245 12.006 14.317 1.00 34.34 ATOM 2089 O GLY 1703 34.977 12.933 13.969 1.00 34.20 ATOM 2090 N VAL 1704 33.552 11.275 13.445 1.00 35.02 ATOM 2092 CA VAL 1704 33.641 11.512 12.007 1.00 32.77 ATOM 2093 CB VAL 1704 33.614 10.176 11.221 1.00 31.32 ATOM 2094 CG1 VAL 1704 33.628 10.435 9.709 1.00 31.46 ATOM 2095 CG2 VAL 1704 34.796 9.297 11.637 1.00 27.62 ATOM 2096 C VAL 1704 32.510 12.410 11.513 1.00 33.35 ATOM 2097 O VAL 1704 31.337 12.070 11.640 1.00 33.94 ATOM 2098 N PRO 1705 32.849 13.589 10.974 1.00 32.43 ATOM 2099 CD PRO 1705 34.181 4.221 10.949 1.00 32.77 ATOM 2100 CA PRO 1705 31.826 14.505 10.472 1.00 33.61 ATOM 2101 CB PRO 1705 32.545 15.853 10.509 1.00 33.21 ATOM 2102 CG PRO 1705 33.935 15.482 10.141 1.00 35.53 ATOM 2103 C PRO 1705 31.395 14.138 9.052 1.00 33.91 ATOM 2104 O PRO 1705 32.113 13.409 8.354 1.00 32.65 ATOM 2105 N VAL 1706 30.255 14.684 8.619 1.00 33.82 ATOM 2107 CA VAL 1706 29.689 14.447 7.280 1.00 33.97 ATOM 2108 CB VAL 1706 28.617 15.513 6.943 1.00 37.41 ATOM 2109 CG1 VAL 1706 28.045 15.282 5.556 1.00 41.12 ATOM 2110 CG2 VAL 1706 27.507 15.484 7.971 1.00 38.89 ATOM 2111 C VAL 1706 30.712 14.428 6.135 1.00 32.32 ATOM 2112 O VAL 1706 30.819 13.450 5.398 1.00 32.58 ATOM 2113 N GLU 1707 31.477 15.504 6.004 1.00 31.15 ATOM 2115 CA GLU 1707 32.478 15.630 4.956 1.00 29.82 ATOM 2116 CB GLU 1707 33.172 16.989 5.048 1.00 30.05 ATOM 2117 C GLU 1707 33.531 14.541 4.959 1.00 28.52 ATOM 2118 O GLU 1707 33.995 14.134 3.896 1.00 30.85 ATOM 2119 N GLU 1708 33.958 14.110 6.143 1.00 28.70 ATOM 2121 CA GLU 1708 34.978 13.073 6.235 1.00 29.50 ATOM 2122 CB GLU 1708 35.590 13.010 7.641 1.00 31.28 ATOM 2123 CG GLU 1708 36.281 14.289 8.103 1.00 41.63 ATOM 2124 CD GLU 1708 37.454 14.718 7.237 1.00 49.91 ATOM 2125 OE1 GLU 1708 38.020 13.876 6.498 1.00 53.57 ATOM 2126 OE2 GLU 1708 37.821 15.916 7.308 1.00 58.45 ATOM 2127 C GLU 1708 34.365 11.730 5.878 1.00 30.00 ATOM 2128 O GLU 1708 35.016 10.874 5.257 1.00 28.43 ATOM 2129 N LEU 1709 33.103 11.559 6.257 1.00 30.08 ATOM 2131 CA LEU 1709 32.392 10.324 5.964 1.00 29.19 ATOM 2132 CB LEU 1709 30.995 10.347 6.592 1.00 28.97 ATOM 2133 CG LEU 1709 30.109 9.186 6.137 1.00 30.66 ATOM 2134 CD1 LEU 1709 30.664 7.866 6.659 1.00 29.24 ATOM 2135 CD2 LEU 1709 28.684 9.403 6.593 1.00 29.29 ATOM 2136 C LEU 1709 32.294 10.130 4.449 1.00 28.26 ATOM 2137 O LEU 1709 32.450 9.011 3.948 1.00 28.86 ATOM 2138 N PHE 1710 32.016 11.220 3.735 1.00 26.86 ATOM 2140 CA PHE 1710 31.903 11.192 2.285 1.00 28.86 ATOM 2141 CB PHE 1710 31.632 12.593 1.743 1.00 31.88 ATOM 2142 CG PHE 1710 30.249 13.095 2.014 1.00 37.62 ATOM 2143 CD1 PHE 1710 29.265 12.247 2.509 1.00 42.63 ATOM 2144 CD2 PHE 1710 29.931 14.424 1.792 1.00 43.53 ATOM 2145 CE1 PHE 1710 27.977 12.718 2.783 1.00 45.99 ATOM 2146 CE2 PHE 1710 28.648 14.905 2.061 1.00 46.25 ATOM 2147 CZ PHE 1710 27.670 14.045 2.559 1.00 44.45 ATOM 2148 C PHE 1710 33.193 10.660 1.681 1.00 30.42 ATOM 2149 O PHE 1710 33.174 9.807 0.792 1.00 29.01 ATOM 2150 N LYS 1711 34.309 11.152 2.212 1.00 30.64 ATOM 2152 CA LYS 1711 35.650 10.762 1.786 1.00 32.89 ATOM 2153 CB LYS 1711 36.670 11.655 2.502 1.00 37.91 ATOM 2154 CG LYS 1711 38.108 11.479 2.088 1.00 42.99 ATOM 2155 CD LYS 1711 38.976 12.528 2.752 1.00 47.45 ATOM 2156 CE LYS 1711 40.380 12.505 2.182 1.00 52.35 ATOM 2157 NZ LYS 1711 41.104 11.272 2.587 1.00 58.47 ATOM 2161 C LYS 1711 35.913 9.273 2.071 1.00 32.23 ATOM 2162 O LYS 1711 36.445 8.559 1.216 1.00 30.79 ATOM 2163 N LEU 1712 35.533 8.807 3.264 1.00 31.37 ATOM 2165 CA LEU 1712 35.704 7.399 3.630 1.00 29.46 ATOM 2166 CB LEU 1712 35.220 7.117 5.065 1.00 28.57 ATOM 2167 CG LEU 1712 36.045 7.662 6.242 1.00 30.18 ATOM 2168 CD1 LEU 17123 35.395 7.349 7.569 1.00 26.92 ATOM 2169 CD2 LEU 1712 37.452 7.083 6.210 1.00 30.88 ATOM 2170 C LEU 1712 34.922 6.539 2.651 1.00 28.99 ATOM 2171 O LEU 1712 35.438 5.551 2.136 1.00 30.73 ATOM 2172 N LEU 1713 33.675 6.915 2.388 1.00 30.13 ATOM 2174 CA LEU 1713 32.851 6.158 1.456 1.00 32.10 ATOM 2175 CB LEU 1713 31.411 6.685 1.443 1.00 35.23 ATOM 2176 CG LEU 1713 30.612 6.292 2.691 1.00 37.47 ATOM 2177 CD1 LEU 1713 29.265 6.982 2.720 1.00 40.85 ATOM 2178 CD2 LEU 1713 30.447 4.788 2.723 1.00 39.61 ATOM 2179 C LEU 1713 33.441 6.147 0.047 1.00 32.70 ATOM 2180 O LEU 1713 33.548 5.090 −0.578 1.00 31.86 ATOM 2181 N LYS 1714 33.859 7.309 −0.444 1.00 32.42 ATOM 2183 CA LYS 1714 34.440 7.387 −1.776 1.00 32.56 ATOM 2184 CB LYS 1714 34.826 8.824 −2.112 1.00 33.02 ATOM 2185 CG LYS 1714 33.640 9.736 −2.297 1.00 35.56 ATOM 2186 CD LYS 1714 32.736 9.235 −3.396 1.00 37.94 ATOM 2187 CE LYS 1714 31.635 10.246 −3.682 1.00 42.57 ATOM 2188 NZ LYS 1714 30.727 9.805 −4.779 1.00 47.40 ATOM 2192 C LYS 1714 35.664 6.488 −1.885 1.00 35.36 ATOM 2193 O LYS 1714 35.927 5.898 −2.937 1.00 36.68 ATOM 2194 N GLU 1715 36.376 6.338 −0.775 1.00 34.51 ATOM 2196 CA GLU 1715 37.577 5.527 −0.749 1.00 35.31 ATOM 2197 CB GLU 1715 38.566 6.125 0.250 1.00 37.07 ATOM 2198 CG GLU 1715 38.967 7.537 −0.163 1.00 43.62 ATOM 2199 CD GLU 1715 39.735 8.310 0.893 1.00 49.75 ATOM 2200 OE1 GLU 1715 39.906 7.814 2.029 1.00 49.71 ATOM 2201 OE2 GLU 1715 40.163 9.442 0.572 1.00 55.13 ATOM 2202 C GLU 1715 37.221 4.048 −0.487 1.00 34.08 ATOM 2203 O GLU 1715 38.259 2.260 −0.438 1.00 34.82 ATOM 2204 N GLY 1716 36.049 3.674 −0.366 1.00 31.53 ATOM 2206 CA GLY 1716 35.695 2.288 −0.133 1.00 27.58 ATOM 2207 C GLY 1716 35.966 1.765 1.262 1.00 28.60 ATOM 2208 O GLY 1716 36.069 0.560 1.464 1.00 27.81 ATOM 2209 N HIS 1717 36.062 2.663 2.236 1.00 29.10 ATOM 2211 CA HIS 1717 36.319 2.263 3.617 1.00 29.30 ATOM 2212 CD HIS 1717 36.501 3.510 4.486 1.00 30.54 ATOM 2213 CG HIS 1717 36.788 3.213 5.930 1.00 32.88 ATOM 2214 CD2 HIS 1717 37.961 3.023 6.586 1.00 32.21 ATOM 2215 ND1 HIS 1717 35.798 3.108 6.881 1.00 34.22 ATOM 2217 CE1 HIS 1717 36.342 2.865 8.061 1.00 31.51 ATOM 2218 NE2 HIS 1717 37.651 2.809 7.907 1.00 31.94 ATOM 2220 C HIS 1717 35.180 1.416 4.183 1.00 28.42 ATOM 2221 O HIS 1717 34.017 1.666 3.885 1.00 30.71 ATOM 2222 N ARG 1718 35.526 0.450 5.028 1.00 27.75 ATOM 2224 CA ARG 1718 34.559 −0.423 5.688 1.00 27.58 ATOM 2225 CN ARG 1718 34.562 −1.813 5.048 1.00 29.07 ATOM 2226 CG ARG 1718 34.078 −1.860 3.597 1.00 28.39 ATOM 2227 CD ARG 1718 32.609 −1.412 3.475 1.00 27.64 ATOM 2228 NE ARG 1718 32.091 −1.467 2.096 1.00 24.37 ATOM 2230 CZ ARG 1718 32.173 −0.476 1.210 1.00 24.26 ATOM 2231 NH1 ARG 1718 32.768 0.668 1.532 1.00 23.98 ATOM 2234 NH2 ARG 1718 31.595 −0.603 0.019 1.00 21.60 ATOM 2237 C ARG 1718 35.005 −0.521 7.148 1.00 30.11 ATOM 2238 O ARG 1718 36.201 −0.623 7.428 1.00 30.60 ATOM 2239 N MET 1719 34.056 −0.430 8.074 1.00 30.69 ATOM 2241 CA MET 1719 34.350 −0.490 9.501 1.00 31.77 ATOM 2242 CB MET 1719 33.072 −0.302 10.335 1.00 34.56 ATOM 2243 CG MET 1719 32.408 1.060 10.194 1.00 36.71 ATOM 2244 SD MET 1719 31.015 1.307 11.314 1.00 38.66 ATOM 2245 CE MET 1719 29.797 0.338 10.544 1.00 36.99 ATOM 2246 C MET 1719 34.998 −1.810 9.854 1.00 30.20 ATOM 2247 O MET 1719 34.802 −2.802 9.169 1.00 31.41 ATOM 2248 N ASP 1720 35.778 −1.809 10.926 1.00 32.49 ATOM 2250 CA ASP 1720 36.473 −3.008 11.385 1.00 33.60 ATOM 2251 CB ASP 1720 37.593 −2.630 12.358 1.00 37.65 ATOM 2252 CG ASP 1720 38.628 −1.688 11.747 1.00 44.69 ATOM 2253 OD1 ASP 1720 38.442 −1.223 10.596 1.00 50.97 ATOM 2254 OD2 ASP 1720 39.632 −1.398 12.443 1.00 48.67 ATOM 2255 C ASP 1720 35.524 −3.977 12.079 1.00 31.26 ATOM 2256 O ASP 1720 34.466 −3.581 12.561 1.00 32.69 ATOM 2257 N LYS 1721 35.943 −5.231 12.191 1.00 32.76 ATOM 2259 CA LYS 1721 35.133 −6.261 12.825 1.00 32.28 ATOM 2260 CB LYS 1721 35.726 −7.649 12.575 1.00 33.63 ATOM 2261 CG LYS 1721 34.854 −8.773 13.125 1.00 35.68 ATOM 2262 CD LYS 1721 35.392 −10.126 12.784 1.00 36.22 ATOM 2263 CE LYS 1721 36.054 −10.749 13.988 1.00 42.65 ATOM 2264 NZ LYS 1721 36.354 −12.189 13.756 1.00 46.15 ATOM 2268 C LYS 1721 35.039 −6.051 14.315 1.00 35.55 ATOM 2269 O LYS 1721 36.064 −5.926 14.986 1.00 37.78 ATOM 2270 N PRO 1722 33.807 −6.017 14.861 1.00 36.91 ATOM 2271 CD PRO 1722 32.504 −6.105 14.179 1.00 34.43 ATOM 2272 CA PRO 1722 33.630 −5.827 16.305 1.00 37.77 ATOM 2273 CB PRO 1722 32.107 −5.846 16.465 1.00 36.32 ATOM 2274 CG PRO 1722 31.603 −5.375 15.122 1.00 34.53 ATOM 2275 C PRO 1722 34.246 −7.026 17.023 1.00 39.31 ATOM 2276 O PRO 1722 34.274 −8.136 16.477 1.00 38.78 ATOM 2277 N SER 1723 34.777 −6.820 18.222 1.00 42.72 ATOM 2279 CA SER 1723 35.336 −7.954 18.940 1.00 45.01 ATOM 2280 CB SER 1723 36.152 −7.508 20.160 1.00 46.88 ATOM 2281 OG SER 1723 35.327 −7.027 21.208 1.00 53.47 ATOM 2283 C SER 1723 34.088 −8.731 19.359 1.00 46.67 ATOM 2284 O SER 1723 32.982 −8.172 19.417 1.00 46.21 ATOM 2285 N ASN 1724 34.237 −10.025 19.590 1.00 47.80 ATOM 2287 CA ASN 1724 33.092 −10.826 19.999 1.00 52.78 ATOM 2288 CB ASN 1724 32.559 −10.319 21.355 1.00 57.86 ATOM 2289 CG ASN 1724 33.679 −10.091 22.370 1.00 61.99 ATOM 2290 OD1 ASN 1724 34.531 −10.959 22.585 1.00 63.17 ATOM 2291 ND2 ASN 1724 33.712 −8.899 22.953 1.00 63.56 ATOM 2294 C ASN 1724 32.015 −10.779 18.893 1.00 51.43 ATOM 2295 O ASN 1724 30.859 −10.423 19.108 1.00 51.56 ATOM 2296 N CYS 1725 32.454 −11.087 17.683 1.00 48.91 ATOM 2298 CA CYS 1725 31.600 −11.136 16.508 1.00 45.62 ATOM 2299 CB CYS 1725 31.526 −9.771 15.811 1.00 44.83 ATOM 2300 SG CYS 1725 30.693 −9.816 14.194 1.00 41.83 ATOM 2301 C CYS 1725 32.341 −12.135 15.640 1.00 42.30 ATOM 2302 O CYS 1725 33.566 −12.045 15.493 1.00 44.63 ATOM 2303 N THR 1726 31.627 −13.134 15.141 1.00 37.46 ATOM 2305 CA THR 1726 32.259 −14.153 14.320 1.00 35.29 ATOM 2306 CB THR 1726 31.339 −15.367 14.132 1.00 33.44 ATOM 2307 OG1 THR 1726 30.109 −14.952 13.523 1.00 34.77 ATOM 2309 CG2 THR 1726 31.070 −16.019 15.454 1.00 30.22 ATOM 2310 C THR 1726 32.668 −13.622 12.963 1.00 33.53 ATOM 2311 O THR 1726 32.158 −12.593 12.518 1.00 32.93 ATOM 2312 N ASN 1727 33.619 −14.294 12.319 1.00 32.72 ATOM 2314 CA ASN 1727 34.030 −13.867 10.983 1.00 35.91 ATOM 2315 CB ASN 1727 35.166 −14.724 10.422 1.00 40.64 ATOM 2316 CG ASN 1727 36.463 −14.533 11.168 1.00 46.52 ATOM 2317 OD1 ASN 1727 37.047 −13.453 11.158 1.00 49.98 ATOM 2318 ND2 ASN 1727 36.931 −15.592 11.814 1.00 49.04 ATOM 2321 C ASN 1727 32.824 −14.006 10.058 1.00 34.27 ATOM 2322 O ASN 1727 32.681 −13.236 9.116 1.00 32.96 ATOM 2323 N GLU 1728 31.969 −14.997 10.326 1.00 32.49 ATOM 2325 CA GLU 1728 30.778 −15.235 9.510 1.00 31.99 ATOM 2326 CB GLU 1728 30.064 −16.504 9.975 1.00 34.15 ATOM 2327 CG GLU 1728 28.836 −16.866 9.156 1.00 35.63 ATOM 2328 CD GLU 1728 28.187 −18.169 9.608 1.00 39.72 ATOM 2329 OE1 GLU 1728 28.200 −18.463 10.824 1.00 42.25 ATOM 2330 OE2 GLU 1728 27.654 −18.896 8.742 1.00 39.87 ATOM 2331 C GLU 1728 29.814 −14.049 9.549 1.00 30.76 ATOM 2332 O GLU 1728 29.309 −13.602 8.512 1.00 29.58 ATOM 2333 N LEU 1729 29.559 −13.544 10.750 1.00 30.01 ATOM 2335 CA LEU 1729 28.670 −12.408 10.911 1.00 30.21 ATOM 2336 CB LEU 1729 28.225 −12.272 12.364 1.00 30.13 ATOM 2337 CG LEU 1729 27.208 −13.350 12.748 1.00 33.61 ATOM 2338 CD1 LEU 1729 27.119 −13.483 14.262 1.00 33.71 ATOM 2339 CD2 LEU 1729 25.844 −13.021 12.139 1.00 30.31 ATOM 2340 C LEU 1729 29.316 −11.133 10.390 1.00 30.26 ATOM 2341 O LEU 1729 28.619 −10.229 9.938 1.00 28.89 ATOM 2342 N TYR 1730 30.648 −11.063 10.435 1.00 28.91 ATOM 2344 CA TYR 1730 31.343 −9.893 9.912 1.00 28.91 ATOM 2345 CB TYR 1730 32.804 −9.861 10.359 1.00 29.09 ATOM 2346 CG TYR 1730 33.537 −8.639 9.857 1.00 30.15 ATOM 2347 CD1 TYR 1730 33.037 −7.358 10.103 1.00 29.97 ATOM 2348 CE1 TYR 1730 33.688 −6.227 9.626 1.00 28.99 ATOM 2349 CD2 TYR 1730 34.716 −8.757 9.119 1.00 29.24 ATOM 2350 CE2 TYR 1730 35.386 −7.620 8.632 1.00 28.25 ATOM 2351 CZ TYR 1730 34.861 −6.362 8.889 1.00 28.41 ATOM 2352 OH TYR 1730 35.485 −5.227 8.405 1.00 31.64 ATOM 2354 C TYR 1730 31.260 −9.943 8.379 1.00 27.10 ATOM 2355 O TYR 1730 31.078 −8.920 7.726 1.00 27.46 ATOM 2356 N MET 1731 31.390 −11.138 7.813 1.00 26.68 ATOM 2358 CA MET 1731 31.298 −11.315 6.372 1.00 28.68 ATOM 2359 CB MET 1731 31.526 −12.778 5.989 1.00 35.43 ATOM 2360 CG MET 1731 31.358 −13.087 4.545 1.00 46.19 ATOM 2361 SD MET 1731 31.441 −14.804 4.064 1.00 60.10 ATOM 2362 CE MET 1731 32.603 −14.550 2.678 1.00 58.31 ATOM 2363 C MET 1731 29.917 −10.858 5.912 1.00 27.42 ATOM 2364 O MET 1731 29.782 −10.227 4.871 1.00 30.80 ATOM 2365 N MET 1732 28.893 −11.191 6.688 1.00 28.53 ATOM 2367 CA MET 1732 27.522 −10.777 6.389 1.00 26.47 ATOM 2368 CB MET 1732 26.562 −11.308 7.458 1.00 25.79 ATOM 2369 CG MET 1732 25.116 −10.838 7.274 1.00 26.01 ATOM 2370 SD MET 1732 24.004 −11.550 8.469 1.00 26.22 ATOM 2371 CE MET 1732 23.787 −13.195 7.783 1.00 23.74 ATOM 2372 C MET 1732 27.445 −9.243 6.319 1.00 25.15 ATOM 2373 O MET 1732 26.886 −8.691 5.379 1.00 25.41 ATOM 2374 N MET 1733 28.024 −8.564 7.308 1.00 26.48 ATOM 2376 CA MET 1733 28.057 −7.104 7.331 1.00 27.09 ATOM 2377 CB MET 1733 28.903 −6.594 8.488 1.00 25.91 ATOM 2378 CG MET 1733 28.235 −6.556 9.824 1.00 31.64 ATOM 2379 SD MET 1733 29.442 −6.111 11.094 1.00 29.59 ATOM 2380 CE MET 1733 28.886 −7.126 12.420 1.00 28.14 ATOM 2381 C MET 1733 28.720 −6.613 6.056 1.00 28.43 ATOM 2382 O MET 1733 28.185 −5.753 5.372 1.00 31.37 ATOM 2383 N ARG 1734 29.891 −7.169 5.747 1.00 28.57 ATOM 2385 CA ARG 1734 30.642 −6.783 4.551 1.00 27.00 ATOM 2386 CB ARG 1734 32.007 −7.488 4.510 1.00 25.98 ATOM 2387 CG ARG 1734 32.927 −7.154 5.707 1.00 28.13 ATOM 2388 CD ARG 1734 33.229 −5.672 5.765 1.00 29.97 ATOM 2389 NE ARG 1734 33.922 −5.256 4.553 1.00 40.49 ATOM 2391 CZ ARG 1734 35.238 −5.361 4.363 1.00 43.95 ATOM 2392 NH1 ARG 1734 36.023 −5.853 5.318 1.00 41.81 ATOM 2395 NH2 ARG 1734 35.760 −5.048 3.184 1.00 46.20 ATOM 2398 C ARG 1734 29.859 −7.037 3.268 1.00 24.57 ATOM 2399 O ARG 1734 29.992 −6.290 2.314 1.00 24.94 ATOM 2400 N ASP 1735 29.071 −8.107 3.235 1.00 24.79 ATOM 2402 CA ASP 1735 28.254 −8.420 2.061 1.00 23.88 ATOM 2403 CB ASP 1735 27.669 −9.830 2.150 1.00 25.95 ATOM 2404 CG ASP 1735 28.724 −10.913 2.024 1.00 27.60 ATOM 2405 OD1 ASP 1735 29.842 −10.632 1.529 1.00 27.75 ATOM 2406 OD2 ASP 1735 28.432 −12.051 2.430 1.00 28.90 ATOM 2407 C ASP 1735 27.139 −7.396 1.941 1.00 22.61 ATOM 2408 O ASP 1735 26.777 −6.996 0.833 1.00 22.66 ATOM 2409 N CYS 1736 26.611 −6.965 3.085 1.00 20.61 ATOM 2411 CA CYS 1736 25.561 −5.952 3.109 1.00 23.63 ATOM 2412 CB CYS 1736 25.007 −5.767 4.534 1.00 21.98 ATOM 2413 SG CYS 1736 23.934 −7.126 5.111 1.00 22.95 ATOM 2414 C CYS 1736 26.129 −4.633 2.599 1.00 23.62 ATOM 2415 O CYS 1736 25.403 −3.797 2.047 1.00 22.15 ATOM 2416 N TRP 1737 27.438 −4.461 2.775 1.00 24.37 ATOM 2418 CA TRP 1737 28.123 −3.247 2.342 1.00 23.77 ATOM 2419 CB TRP 1737 29.162 −2.810 3.371 1.00 19.38 ATOM 2420 CG TRP 1737 28.601 −2.520 4.718 1.00 21.62 ATOM 2421 CD2 TRP 1737 29.268 −2.688 5.971 1.00 24.81 ATOM 2422 CE2 TRP 1737 28.371 −2.278 6.980 1.00 25.95 ATOM 2423 CE3 TRP 1737 30.534 −3.165 6.340 1.00 29.02 ATOM 2424 CD1 TRP 1737 27.359 −2.024 5.007 1.00 23.21 ATOM 2425 NE1 TRP 1737 27.213 −1.876 6.362 1.00 21.80 ATOM 2427 CZ2 TRP 1737 28.710 −2.305 8.347 1.00 26.68 ATOM 2428 CZ3 TRP 1737 30.873 −3.198 7.699 1.00 31.06 ATOM 2429 CH2 TRP 1737 29.959 −2.774 8.685 1.00 30.18 ATOM 2430 C TRP 1737 28.788 −3.372 0.978 1.00 24.88 ATOM 2431 O TRP 1737 29.737 −2.646 0.689 1.00 25.11 ATOM 2432 N HIS 1738 28.303 −4.278 0.132 1.00 25.27 ATOM 2434 CA HIS 1738 28.888 −4.406 −1.191 1.00 24.27 ATOM 2435 CB HIS 1738 28.280 −5.573 −1.986 1.00 25.24 ATOM 2436 CG HIS 1738 29.179 −6.073 −3.081 1.00 26.28 ATOM 2437 CD2 HIS 1738 29.727 −5.437 −4.147 1.00 25.67 ATOM 2438 ND1 HIS 1738 29.697 −7.352 −3.098 1.00 27.55 ATOM 2440 CE1 HIS 1738 30.528 −7.478 −4.117 1.00 27.51 ATOM 2441 NE2 HIS 1738 30.564 −6.329 −4.770 1.00 30.93 ATOM 2443 C HIS 1738 28.715 −3.087 −1.953 1.00 25.59 ATOM 2444 O HIS 1738 27.659 −2.451 −1.905 1.00 22.01 ATOM 2445 N ALA 1739 29.784 −2.651 −2.612 1.00 23.84 ATOM 2447 CA ALA 1739 29.759 −1.418 −3.388 1.00 24.93 ATOM 2448 CB ALA 1739 31.131 −1.177 −4.024 1.00 26.39 ATOM 2449 C ALA 1739 28.671 −1.508 −4.462 1.00 25.35 ATOM 2450 O ALA 1739 27.963 −0.535 −4.727 1.00 28.20 ATOM 2451 N VAL 1740 28.543 −2.680 −5.073 1.00 22.68 ATOM 2453 CA VAL 1740 27.528 −2.904 −6.101 1.00 26.46 ATOM 2454 CB VAL 1740 27.995 −3.968 −7.117 1.00 29.70 ATOM 2455 CG1 VAL 1740 27.063 −4.003 −8.334 1.00 26.01 ATOM 2456 CG2 VAL 1740 29.433 −3.686 −7.537 1.00 31.22 ATOM 2457 C VAL 1740 26.213 −3.358 −5.443 1.00 25.07 ATOM 2458 O VAL 1740 26.138 −4.474 −4.903 1.00 23.55 ATOM 2459 N PRO 1741 25.155 −2.519 −5.514 1.00 25.30 ATOM 2460 CD PRO 1741 25.133 −1.190 −6.153 1.00 22.43 ATOM 2461 CA PRO 1741 23.844 −2.833 −4.921 1.00 24.09 ATOM 2462 CB PRO 1741 22.962 −1.675 −5.402 1.00 23.12 ATOM 2463 CG PRO 1741 23.928 −0.527 −5.491 1.00 22.04 ATOM 2464 C PRO 1741 23.272 −4.191 −5.313 1.00 22.18 ATOM 2465 O PRO 1741 22.727 −4.900 −4.466 1.00 21.23 ATOM 2466 N SER 1742 23.437 −4.570 −6.580 1.00 23.87 ATOM 2468 CA SER 1742 22.928 −5.847 −7.088 1.00 24.36 ATOM 2469 CB SER 1742 23.071 −5.907 −8.612 1.00 27.39 ATOM 2470 OG SER 1742 24.436 −6.025 −8.986 1.00 29.25 ATOM 2472 C SER 1742 23.636 −7.058 −6.488 1.00 23.96 ATOM 2473 O SER 1742 23.145 −8.179 −6.575 1.00 24.30 ATOM 2474 N GLN 1743 24.810 −6.839 −5.915 1.00 24.39 ATOM 2476 CA GLN 1743 25.558 −7.934 −5.345 1.00 23.15 ATOM 2477 CB GLN 1743 27.046 −7.755 −5.638 1.00 23.83 ATOM 2478 CG GLN 1743 27.359 −7.784 −7.126 1.00 22.84 ATOM 2479 CD GLN 1743 26.816 −9.036 −7.808 1.00 24.20 ATOM 2480 OE1 GLN 1743 27.318 −10.135 −7.590 1.00 21.50 ATOM 2481 NE2 GLN 1743 25.775 −8.871 −8.628 1.00 22.45 ATOM 2484 C GLN 1743 25.309 −8.171 −3.868 1.00 23.12 ATOM 2485 O GLN 1743 25.816 −9.135 −3.317 1.00 24.96 ATOM 2486 N ARG 1744 24.557 −7.280 −3.225 1.00 23.67 ATOM 2488 CA ARG 1744 24.242 −7.424 −1.806 1.00 22.11 ATOM 2489 CB ARG 1744 23.699 −6.110 −1.231 1.00 19.70 ATOM 2490 CG ARG 1744 24.672 −4.959 −1.338 1.00 21.26 ATOM 2491 CD ARG 1744 24.049 −3.640 −0.890 1.00 20.68 ATOM 2492 NE ARG 1744 24.923 −2.552 −1.305 1.00 25.21 ATOM 2494 CZ ARG 1744 24.540 −1.313 −1.583 1.00 24.30 ATOM 2495 NH1 ARG 1744 23.257 −0.955 −1.481 1.00 22.04 ATOM 2498 NH2 ARG 1744 25.450 −0.448 −2.036 1.00 21.29 ATOM 2501 C ARG 1744 23.184 −8.505 −1.640 1.00 22.53 ATOM 2502 O ARG 1744 22.437 −8.800 −2.588 1.00 23.08 ATOM 2503 N PRO 1745 23.162 −9.170 −0.467 1.00 20.76 ATOM 2504 CD PRO 1745 24.087 −9.078 0.681 1.00 21.71 ATOM 2505 CA PRO 1745 22.160 −10.207 −0.243 1.00 22.34 ATOM 2506 CB PRO 1745 22.632 −10.859 1.057 1.00 20.58 ATOM 2507 CG PRO 1745 23.298 −9.727 1.783 1.00 20.36 ATOM 2508 C PRO 1745 20.814 −9.512 −0.048 1.00 23.62 ATOM 2509 O PRO 1745 20.759 −8.318 0.255 1.00 25.29 ATOM 2510 N THR 1746 19.731 −10.235 −0.275 1.00 23.39 ATOM 2512 CA THR 1746 18.404 −9.675 −0.080 1.00 22.77 ATOM 2513 CB THR 1746 17.386 −10.368 −1.004 1.00 23.24 ATOM 2514 OG1 THR 1746 27.409 −11.783 −0.763 1.00 23.11 ATOM 2516 CG2 THR 1746 17.724 −10.103 −2.475 1.00 24.96 ATOM 2517 C THR 1746 18.009 −9.954 1.365 1.00 24.98 ATOM 2518 O THR 1746 18.664 −10.758 2.043 1.00 24.30 ATOM 2519 N PHE 1747 16.944 −9.318 1.853 1.00 24.95 ATOM 2521 CA PHE 1747 16.501 −9.596 3.221 1.00 25.16 ATOM 2522 CB PHE 1747 15.395 −8.628 3.661 1.00 23.64 ATOM 2523 CG PHE 1747 15.916 −7.283 4.089 1.00 24.34 ATOM 2524 CD1 PHE 1747 16.715 −7.167 5.226 1.00 21.21 ATOM 2525 CD2 PHE 1747 15.649 −6.137 3.334 1.00 21.42 ATOM 2526 CE1 PHE 1747 17.252 −5.932 5.597 1.00 20.99 ATOM 2527 CE2 PHE 1747 16.178 −4.907 3.699 1.00 20.36 ATOM 2528 CZ PHE 1747 16.985 −4.807 4.840 1.00 19.30 ATOM 2529 C PHE 1747 16.034 −11.049 3.311 1.00 23.57 ATOM 2530 O PHE 1747 16.182 −11.702 4.344 1.00 25.32 ATOM 2531 N LYS 1748 15.520 −11.573 2.202 1.00 23.19 ATOM 2533 CA LYS 1748 15.066 −12.958 2.167 1.00 23.67 ATOM 2534 CB LYS 1748 14.462 −13.285 0.799 1.00 26.67 ATOM 2535 CG LYS 1748 14.018 −14.739 0.622 1.00 30.49 ATOM 2536 CD LYS 1748 13.642 −4.996 −0.837 1.00 38.98 ATOM 2537 CE LYS 1748 13.182 −16.432 −1.087 1.00 44.52 ATOM 2538 NZ LYS 1748 11.997 −16.790 −0.245 1.00 52.75 ATOM 2542 C LYS 1748 16.264 −13.865 2.445 1.00 25.65 ATOM 2543 O LYS 1748 16.184 −14.776 3.270 1.00 27.19 ATOM 2544 N GLN 1749 17.378 −13.603 1.762 1.00 24.56 ATOM 2546 CA GLN 1749 18.588 −14.397 1.950 1.00 26.33 ATOM 2547 CB GLN 1749 19.702 −13.953 0.993 1.00 27.97 ATOM 2548 CG GLN 1749 19.416 −14.066 −0.484 1.00 37.31 ATOM 2549 CD GLN 1749 20.518 −13.415 −1.315 1.00 40.24 ATOM 2550 OE1 GLN 1749 20.296 −12.408 −1.970 1.00 38.83 ATOM 2551 NE2 GLN 1749 21.726 −13.983 −1.259 1.00 47.83 ATOM 2554 C GLN 1749 19.099 −14.223 3.377 1.00 23.92 ATOM 2555 O GLN 1749 19.459 −15.196 4.040 1.00 25.27 ATOM 2556 N LEU 1750 19.155 −12.976 3.829 1.00 23.12 ATOM 2558 CA LEU 1750 19.641 −12.662 5.175 1.00 24.34 ATOM 2559 CB LEU 1750 19.607 −11.149 5.427 1.00 23.08 ATOM 2560 CG LEU 1750 20.633 −10.311 4.665 1.00 23.84 ATOM 2561 CD1 LEU 1750 20.274 −8.806 4.724 1.00 22.10 ATOM 2562 CD2 LEU 1750 22.013 −10.586 5.246 1.00 24.91 ATOM 2563 C LEU 1750 18.840 −13.400 6.236 1.00 27.40 ATOM 2564 O LEU 1750 29.408 −13.915 7.211 1.00 27.11 ATOM 2565 N VAL 1751 17.527 −13.482 6.031 1.00 26.83 ATOM 2567 CA VAL 1751 16.665 −14.174 6.970 1.00 25.31 ATOM 2568 CB VAL 1751 15.176 −13.994 6.599 1.00 25.87 ATOM 2569 CG1 VAL 1751 14.304 −14.975 7.382 1.00 28.43 ATOM 2570 CG2 VAL 1751 14.746 −12.593 6.934 1.00 21.52 ATOM 2571 C VAL 1751 17.047 −15.642 7.025 1.00 25.87 ATOM 2572 O VAL 1751 17.178 −16.218 8.106 1.00 23.41 ATOM 2573 N GLU 1752 17.253 −16.243 5.858 1.00 29.98 ATOM 2575 CA GLU 1752 17.631 −17.651 5.799 1.00 33.12 ATOM 2576 CB GLU 1752 17.653 −18.134 4.346 1.00 35.99 ATOM 2577 CG GLU 1752 16.284 −18.077 3.670 1.00 43.58 ATOM 2578 CD GLU 1752 16.300 −18.575 2.230 1.00 48.64 ATOM 2579 OE1 GLU 1752 15.453 −18.124 1.431 1.00 48.99 ATOM 2580 OE2 GLU 1752 17.157 −19.426 1.902 1.00 55.41 ATOM 2581 C GLU 1752 18.995 −17.891 6.467 1.00 33.15 ATOM 2582 O GLU 1752 19.173 −18.847 7.236 1.00 30.71 ATOM 2583 N ASP 1753 19.951 −17.011 6.186 1.00 31.12 ATOM 2585 CA ASP 1753 21.279 −17.131 6.770 1.00 30.51 ATOM 2586 CB ASP 1753 22.243 −16.108 6.155 1.00 29.15 ATOM 2587 CG ASP 1753 22.488 −16.344 4.672 1.00 33.53 ATOM 2588 OD1 ASP 1753 22.361 −17.494 4.215 1.00 34.92 ATOM 2589 OD2 ASP 1753 22.815 −15.371 3.955 1.00 38.26 ATOM 2590 C ASP 1753 21.215 −16.968 8.287 1.00 28.54 ATOM 2591 O ASP 1753 21.739 −17.800 9.025 1.00 28.95 ATOM 2592 N LEU 1754 20.537 −15.926 8.753 1.00 27.25 ATOM 2594 CA LEU 1754 20.421 −15.673 10.193 1.00 28.08 ATOM 2595 CB LEU 1754 19.754 −14.328 10.455 1.00 23.31 ATOM 2596 CG LEU 1754 20.733 −13.199 10.160 1.00 24.47 ATOM 2597 CD1 LEU 1754 20.007 −11.863 10.094 1.00 19.58 ATOM 2598 CD2 LEU 1754 21.846 −13.207 11.216 1.00 21.17 ATOM 25g9 C LEU 1754 19.688 −16.789 10.921 1.00 31.61 ATOM 2600 O LEU 1754 20.037 −17.135 12.048 1.00 32.64 ATOM 2601 N ASP 1755 18.690 −17.367 10.259 1.00 32.61 ATOM 2603 CA ASP 1755 17.931 −18.460 10.833 1.00 34.20 ATOM 2604 CB ASP 1755 16.823 −18.883 9.872 1.00 37.70 ATOM 2605 CG ASP 1755 15.808 −19.780 10.526 1.00 44.27 ATOM 2606 OD1 ASP 1755 15.445 −19.521 11.692 1.00 47.16 ATOM 2607 OD2 ASP 1755 15.370 −20.745 9.876 1.00 51.35 ATOM 2608 C ASP 1755 18.894 −19.616 11.073 1.00 34.63 ATOM 2609 O ASP 1755 18.858 −20.273 12.119 1.00 36.24 ATOM 2610 N ARG 1756 19.782 −19.826 10.108 1.00 32.60 ATOM 2612 CA ARG 1756 20.784 −20.870 10.190 1.00 33.69 ATOM 2613 CB ARG 1756 21.548 −20.939 8.867 1.00 35.42 ATOM 2614 CG ARG 1756 22.639 −22.003 8.800 1.00 40.87 ATOM 2615 CD ARG 1756 23.212 −22.094 7.395 1.00 42.73 ATOM 2616 NE ARG 1756 23.739 −20.813 6.926 1.00 48.45 ATOM 2618 CZ ARG 1756 24.882 −20.274 7.340 1.00 49.90 ATOM 2619 NH1 ARG 1756 25.634 −20.905 8.243 1.00 49.63 ATOM 2622 NH2 ARG 1756 25.276 −19.105 6.844 1.00 50.86 ATOM 2625 C ARG 1756 21.748 −20.598 11.345 1.00 34.78 ATOM 2626 O ARG 1756 21.929 −21.436 12.228 1.00 36.24 ATOM 2627 N ILE 1757 22.325 −19.402 11.363 1.00 35.35 ATOM 2629 CA ILE 1757 23.281 −19.018 12.392 1.00 35.54 ATOM 2630 CB ILE 1757 23.905 −17.631 12.103 1.00 34.99 ATOM 2631 CG2 ILE 1757 24.955 −17.303 13.159 1.00 32.06 ATOM 2632 CG1 ILE 1757 24.547 −17.626 10.711 1.00 33.77 ATOM 2633 CD1 ILE 1757 24.908 −16.247 10.185 1.00 31.44 ATOM 2634 C ILE 1757 22.698 −19.036 13.803 1.00 36.49 ATOM 2635 O ILE 1757 23.337 −19.548 14.716 1.00 36.40 ATOM 2636 N VAL 1758 21.487 −18.515 13.988 1.00 36.91 ATOM 2638 CA VAL 1758 20.881 −18.498 15.322 1.00 38.68 ATOM 2639 CB VAL 1758 19.425 −17.962 15.312 1.00 37.77 ATOM 2640 CG1 VAL 1758 18.806 −18.059 16.708 1.00 38.39 ATOM 2641 CG2 VAL 1758 19.392 −16.524 14.854 1.00 36.69 ATOM 2642 C VAL 1758 20.891 −19.908 15.895 1.00 41.38 ATOM 2643 O VAL 1758 21.405 −20.138 16.997 1.00 42.41 ATOM 2644 N ALA 1759 20.379 −20.851 15.111 1.00 40.59 ATOM 2646 CA ALA 1759 20.325 −22.247 15.508 1.00 40.84 ATOM 2647 CB ALA 1759 19.741 −23.074 14.384 1.00 40.20 ATOM 2648 C ALA 1759 21.703 −22.787 15.897 1.00 42.52 ATOM 2649 0 ALA 1759 21.822 −23.594 16.809 1.00 44.78 ATOM 2650 N LEU 1760 22.740 −22.339 15.208 1.00 43.16 ATOM 2652 CA LEU 1760 24.095 −22.800 15.493 1.00 46.98 ATOM 2653 CB LEU 1760 24.921 −22.761 14.203 1.00 47.66 ATOM 2654 CG LEU 1760 24.286 −23.545 13.060 1.00 52.77 ATOM 2655 CD1 LEU 1760 24.973 −23.222 11.745 1.00 56.58 ATOM 2656 CD2 LEU 1760 24.343 −25.038 13.369 1.00 53.06 ATOM 2657 C LEU 1760 24.811 −21.986 16.573 1.00 47.43 ATOM 2658 O LEU 1760 25.917 −22.335 16.989 1.00 46.58 ATOM 2659 N THR 1761 24.183 −20.914 17.034 1.00 48.65 ATOM 2661 CA THR 1761 24.814 −20.055 18.021 1.00 49.69 ATOM 2662 CB THR 1761 24.382 −18.570 17.831 1.00 50.15 ATOM 2663 OG1 THR 1761 24.783 −18.127 16.529 1.00 49.87 ATOM 2665 CG2 THR 1761 25.063 −17.671 18.843 1.00 48.64 ATOM 2666 C THR 1761 24.673 −20.497 19.475 1.00 50.33 ATOM 2667 O THR 1761 23.584 −20.825 19.947 1.00 48.81 ATOM 2668 N SER 1762 25.811 −20.511 20.166 1.00 50.25 ATOM 2670 CA SER 1762 25.891 −20.890 21.566 1.00 50.98 ATOM 2671 CB SER 1762 27.362 −20.887 22.002 1.00 54.71 ATOM 2672 OG SER 1762 27.537 −21.423 23.308 1.00 57.99 ATOM 2674 C SER 1762 25.083 −19.914 22.425 1.00 49.39 ATOM 2675 O SER 1762 25.297 −18.694 22.370 1.00 48.00 ATOM 3474 N SER 461 79.623 25.766 14.533 1.00 48.84 ATOM 3476 CA SER 461 79.566 24.645 13.593 1.00 46.93 ATOM 3477 CB SER 461 78.276 23.838 13.809 1.00 46.66 ATOM 3478 C SER 461 79.676 25.114 12.138 1.00 43.02 ATOM 3479 O SER 461 79.692 24.301 11.210 1.00 40.19 ATOM 3480 N GLU 462 79.791 26.427 11.956 1.00 41.48 ATOM 3482 CA GLU 462 79.904 27.034 10.628 1.00 39.59 ATOM 3483 CB GLU 462 80.021 28.560 10.744 1.00 40.66 ATOM 3484 C GLU 462 81.054 26.480 9.796 1.00 36.60 ATOM 3485 O GLU 462 80.852 26.121 8.641 1.00 35.10 ATOM 3486 N TYR 463 82.252 26.416 10.380 1.00 36.07 ATOM 3488 CA TYR 463 83.430 25.916 9.673 1.00 35.60 ATOM 3489 CB TYR 463 84.597 26.906 9.755 1.00 38.15 ATOM 3490 CG TYR 463 84.372 28.104 8.861 1.00 44.08 ATOM 3491 CD1 TYR 463 84.137 29.368 9.406 1.00 44.99 ATOM 3492 CE1 TYR 463 83.833 30.451 8.593 1.00 46.88 ATOM 3493 CD2 TYR 463 84.305 27.959 7.464 1.00 43.95 ATOM 3494 CE2 TYR 463 84.003 29.044 6.642 1.00 41.86 ATOM 3495 CZ TYR 463 83.768 30.282 7.215 1.00 43.89 ATOM 3496 OH TYR 463 83.468 31.364 6.431 1.00 44.37 ATOM 3498 C TYR 463 83.903 24.520 10.014 1.00 33.90 ATOM 3499 O TYR 463 84.440 23.828 9.147 1.00 33.90 ATOM 3500 N GLU 464 83.742 24.098 11.260 1.00 32.81 ATOM 3502 CA GLU 464 84.167 22.753 11.633 1.00 34.64 ATOM 3503 CB GLU 464 85.663 22.727 11.919 1.00 37.48 ATOM 3504 CG GUU 464 86.075 23.633 13.049 1.00 45.48 ATOM 3505 CD GLU 464 87.552 23.987 13.015 1.00 55.80 ATOM 3506 CE1 GLU 464 87.920 24.996 13.659 1.00 61.78 ATOM 3507 OE2 GLU 464 88.344 23.271 12.351 1.00 58.34 ATOM 3508 C GLU 464 83.426 22.296 12.858 1.00 33.05 ATOM 3509 O GLU 464 83.083 23.119 13.705 1.00 34.54 ATOM 3510 N LEU 465 83.147 21.001 12.943 1.00 32.59 ATOM 3512 CA LEU 465 82.462 20.463 14.114 1.00 33.74 ATOM 3513 CB LEU 465 81.484 19.341 13.747 1.00 31.20 ATOM 3514 CG LEU 465 80.510 19.433 12.577 1.00 32.77 ATOM 3515 CD1 LEU 465 79.355 18.492 12.858 1.00 26.22 ATOM 3516 CD2 LEU 465 80.021 20.846 12.359 1.00 31.59 ATOM 3517 C LEU 465 83.511 19.889 15.059 1.00 35.64 ATOM 3518 O LEU 465 84.641 19.574 14.642 1.00 33.77 ATOM 3519 N PRO 466 83.150 19.734 16.349 1.00 36.71 ATOM 3520 CD PRO 466 81.865 20.104 16.967 1.00 36.97 ATOM 3521 CA PRO 466 84.074 19.185 17.346 1.00 36.17 ATOM 3522 CB PRO 466 83.247 19.196 18.626 1.00 36.83 ATOM 3523 CG PRO 466 82.274 20.326 18.394 1.00 40.80 ATOM 3524 C PRO 466 84.419 17.765 16.950 1.00 37.39 ATOM 3525 O PRO 466 83.626 17.077 16.297 1.00 34.71 ATOM 3526 N GLU 467 85.611 17.330 17.315 1.00 38.40 ATOM 3528 CA GLU 467 86.030 15.987 16.976 1.00 42.59 ATOM 3529 CB GLU 467 87.493 15.987 16.540 1.00 49.21 ATOM 3530 CG GLU 467 87.922 14.682 15.891 1.00 58.93 ATOM 3531 CD GLU 467 89.276 14.769 15.213 1.00 64.76 ATOM 3532 OE1 GLU 467 90.013 15.767 15.426 1.00 63.57 ATOM 3533 OE2 GLU 467 89.592 13.823 14.458 1.00 69.03 ATOM 3534 C GLU 467 85.825 15.037 18.146 1.00 40.74 ATOM 3535 O GLU 467 85.938 15.430 19.309 1.00 41.52 ATOM 3536 N ASP 468 85.472 13.802 17.831 1.00 38.57 ATOM 3538 CA ASP 468 85.273 12.776 18.851 1.00 40.86 ATOM 3539 CB ASP 468 83.793 12.640 19.224 1.00 40.27 ATOM 3540 CG ASP 468 83.566 11.697 20.397 1.00 41.36 ATOM 3541 OD1 ASP 468 82.429 11.670 20.919 1.00 42.50 ATOM 3542 OD2 ASP 468 84.514 10.992 20.807 1.00 38.55 ATOM 3543 C ASP 468 85.803 11.470 18.278 1.00 40.75 ATOM 3544 O ASP 468 85.068 10.701 17.650 1.00 41.80 ATOM 3545 N PRO 469 87.100 11.209 18.481 1.00 41.71 ATOM 3546 CD PRO 469 88.001 12.062 19.276 1.00 41.87 ATOM 3547 CA PRO 469 87.801 10.011 18.012 1.00 40.07 ATOM 3548 CB PRO 469 89.091 10.042 18.831 1.00 40.42 ATOM 3549 CG PRO 469 89.366 11.505 18.938 1.00 39.42 ATOM 3550 C PRO 469 87.033 8.720 18.260 1.00 41.00 ATOM 3551 O PRO 469 87.032 7.822 17.414 1.00 41.75 ATOM 3552 N ARG 470 86.361 8.639 19.411 1.00 40.70 ATOM 3554 CA ARG 470 85.600 7.446 19.779 1.00 41.03 ATOM 3555 CB ARH 470 84.827 7.677 21.075 1.00 44.18 ATOM 3556 CG ARG 470 85.628 8.240 22.218 1.00 47.89 ATOM 3557 CD ARG 470 84.719 8.518 23.400 1.00 50.56 ATOM 3558 NE ARG 470 83.576 9.345 23.023 1.00 51.20 ATOM 3560 CZ ARG 470 82.695 9.845 23.881 1.00 52.24 ATOM 3561 NH1 ARG 470 82.818 9.608 25.183 1.00 51.31 ATOM 3564 NH2 ARG 470 81.672 10.564 23.432 1.00 52.73 ATOM 3567 C ARG 470 84.596 7.004 18.723 1.00 39.03 ATOM 3568 O ARG 470 84.401 5.813 18.518 1.00 40.72 ATOM 3569 N TRP 471 83.972 7.965 18.050 1.00 37.77 ATOM 3571 CA TRP 471 82.948 7.656 17.059 1.00 36.73 ATOM 3572 CB TRP 471 81.672 8.401 17.432 1.00 35.05 ATOM 3573 CG TRP 471 81.044 7.862 18.673 1.00 34.85 ATOM 3574 CD2 TRP 471 80.235 3.687 18.766 1.00 34.96 ATOM 3575 CE2 TRP 471 19.831 6.564 20.116 1.00 35.12 ATOM 3576 CE3 TRP 471 79.810 5.721 17.838 1.00 33.25 ATOM 3577 CD1 TRP 471 81.306 8.390 19.933 1.00 29.97 ATOM 3578 NE1 TRP 471 80.377 7.616 20.805 1.00 32.18 ATOM 3580 CZ2 TRP 471 79.017 5.512 20.560 1.00 33.98 ATOM 3581 CZ3 TRP 471 79.002 4.673 18.282 1.00 33.71 ATOM 3582 CH2 TRP 471 78.618 4.580 19.632 1.00 33.28 ATOM 3583 C TRP 471 83.275 7.930 15.599 1.00 37.27 ATOM 3584 O TRP 471 82.580 7.445 14.695 1.00 36.61 ATOM 3585 N GLU 472 84.341 8.680 15.361 1.00 37.93 ATOM 3587 CA GLU 472 84.706 9.054 14.004 1.00 37.08 ATOM 3588 CB GLU 472 85.865 10.049 14.045 1.00 36.30 ATOM 3589 CG GLU 472 86.026 10.851 12.773 1.00 33.51 ATOM 3590 CD GLU 472 84.931 11.895 12.580 1.00 33.80 ATOM 3591 OE1 GLU 472 84.385 12.408 13.581 1.00 35.19 ATOM 3592 OE2 GLU 472 84.641 12.226 11.412 1.00 32.51 ATOM 3593 C GLU 472 85.021 7.923 13.032 1.00 37.88 ATOM 3594 O GLU 472 85.774 7.000 13.351 1.00 38.20 ATOM 3595 N LEU 473 84.422 7.992 11.846 1.00 37.55 ATOM 3597 CA LEU 473 84.678 7.004 10.813 1.00 36.93 ATOM 3598 CB LEU 473 83.404 6.244 10.443 1.00 37.08 ATOM 3599 CG LEU 473 83.680 5.086 9.470 1.00 39.14 ATOM 3600 CD1 LEU 473 84.196 3.877 10.250 1.00 38.39 ATOM 3601 CD2 LEU 473 82.433 4.716 8.672 1.00 39.46 ATOM 3602 C LEU 473 85.207 7.732 9.577 1.00 38.52 ATOM 3603 O LEU 473 84.660 8.764 9.182 1.00 38.67 ATOM 3604 N PRO 474 86.334 7.259 9.005 1.00 39.02 ATOM 3605 CD PRO 474 87.259 6.259 9.571 1.00 38.39 ATOM 3606 CA PRO 474 86.918 7.877 7.809 1.00 38.24 ATOM 3607 CB PRO 474 88.188 7.049 7.590 1.00 38.40 ATOM 3608 CG PRO 474 88.580 6.680 8.979 1.00 35.50 ATOM 3609 C PRO 474 85.942 7.727 6.642 1.00 37.56 ATOM 3610 O PRO 474 85.415 6.641 6.400 1.00 37.88 ATOM 3611 N ARG 475 85.720 8.809 5.907 1.00 37.73 ATOM 3613 CA ARG 475 84.779 8.790 4.795 1.00 40.01 ATOM 3614 CB ARG 475 84.655 10.183 4.182 1.00 38.31 ATOM 3615 CG ARG 475 84.217 11.236 5.198 1.00 35.15 ATOM 3616 CD ARG 475 84.069 12.631 4.586 1.00 33.92 ATOM 3617 NE ARG 475 83.718 13.603 5.616 1.00 30.45 ATOM 3619 CZ ARG 475 82.475 13.880 5.993 1.00 26.48 ATOM 3620 NH1 ARG 475 81.444 13.284 5.407 1.00 24.80 ATOM 3623 NH2 ARG 475 82.271 14.650 7.056 1.00 25.16 ATOM 3626 C ARG 475 85.054 7.735 3.728 1.00 42.18 ATOM 3627 O ARG 475 84.125 7.197 3.128 1.00 41.43 ATOM 3628 N ASP 476 86.322 7.391 3.535 1.00 45.44 ATOM 3630 CA ASP 476 86.676 6.387 2.541 1.00 49.80 ATOM 3631 CB ASP 476 88.192 6.343 2.329 1.00 50.95 ATOM 3632 CG ASP 476 88.944 5.975 3.585 1.00 53.89 ATOM 3633 OD1 ASP 476 89.303 4.789 3.731 1.00 59.71 ATOM 3634 OD2 ASP 476 89.176 6.867 4.427 1.00 57.39 ATOM 3635 C ASP 476 86.149 5.010 2.950 1.00 51.23 ATOM 3636 O ASP 476 86.051 4.102 2.121 1.00 53.54 ATOM 3637 N ARG 477 85.814 4.864 4.230 1.00 50.49 ATOM 3639 CA ARG 477 85.285 3.610 4.753 1.00 49.32 ATOM 3640 CB ARG 477 85.834 3.364 6.152 1.00 49.79 ATOM 3641 CG ARG 477 87.237 2.806 6.112 1.00 53.06 ATOM 3642 CD ARG 477 87.960 2.981 7.420 1.00 56.76 ATOM 3643 NE ARG 477 87.310 2.293 8.529 1.00 59.35 ATOM 3645 CZ ARG 477 87.728 2.371 9.789 1.00 62.23 ATOM 3646 NH1 ARG 477 88.793 3.103 10.101 1.00 63.66 ATOM 3649 NH2 ARG 477 87.067 1.741 10.745 1.00 64.35 ATOM 3652 C ARG 477 83.755 3.547 4.750 1.00 48.04 ATOM 3653 O ARG 477 83.160 2.693 5.404 1.00 48.09 ATOM 3654 N LEU 478 83.129 4.412 3.958 1.00 45.38 AtOM 3656 CA LEU 478 81.685 4.469 3.870 1.00 41.60 ATOM 3657 CB LEU 478 81.168 5.570 4.790 1.00 38.39 ATOM 3658 CG LEU 478 79.651 5.699 4.894 1.00 36.38 ATOM 3659 CD1 LEU 478 79.113 4.595 5.802 1.00 33.98 ATOM 3660 CD2 LEU 478 79.293 7.068 5.441 1.00 40.06 ATOM 3661 C LEU 478 81.279 4.774 2.433 1.00 41.92 ATOM 3662 O LEU 478 81.696 5.780 1.870 1.00 43.99 ATOM 3663 N VAL 479 80.466 3.904 1.844 1.00 42.29 ATOM 3665 CA VAL 479 79.992 4.082 0.471 1.00 41.07 ATOM 3666 CB VAL 479 80.227 2.816 −0.397 1.00 41.13 ATOM 3667 CG1 VAL 479 79.719 3.057 −1.810 1.00 40.19 ATOM 3668 CG2 VAL 479 81.700 2.448 −0.420 1.00 41.36 ATOM 3669 C VAL 479 78.500 4.345 0.540 1.00 40.44 ATOM 3670 O VAL 479 77.719 3.451 0.885 1.00 39.86 ATOM 3671 N LEU 480 78.112 5.582 0.253 1.00 41.37 ATOM 3673 CA LEU 480 76.706 5.973 0.293 1.00 41.63 ATOM 3674 CB LEU 480 76.568 7.492 0.166 1.00 39.91 ATOM 3675 CG LEU 480 77.236 8.332 1.261 1.00 39.23 ATOM 3676 CD1 LEU 480 76.890 9.800 1.039 1.00 37.73 ATOM 3677 CD2 LEU 480 76.791 7.877 2.647 1.00 35.18 ATOM 3678 C LEU 480 75.899 5.273 −0.788 1.00 42.21 ATOM 3679 O LEU 480 76.395 5.048 −1.890 1.00 45.27 ATOM 3680 N GLY 481 74.650 4.947 −0.476 1.00 41.51 ATOM 3682 CA GLY 481 73.812 4.257 −1.433 1.00 40.19 ATOM 3683 C GLY 481 72.446 4.872 −1.640 1.00 41.58 ATOM 3684 O GLY 481 72.262 6.091 −1.550 1.00 41.35 ATOM 3685 N LYS 482 71.474 4.009 −1.908 1.00 42.65 ATOM 3687 CA LYS 482 70.105 4.429 −2.166 1.00 44.17 ATOM 3688 CB LYS 482 69.240 3.221 −2.542 1.00 45.66 ATOM 3689 C LYS 482 69.475 5.148 −0.994 1.00 44.86 ATOM 3690 O LYS 482 69.638 4.752 0.155 1.00 45.23 ATOM 3691 N PRO 483 68.749 6.234 −1.273 1.00 45.94 ATOM 3692 CD PRO 483 68.518 6.880 −2.576 1.00 46.96 ATOM 3693 CA PRO 483 68.099 6.983 −0.206 1.00 47.79 ATOM 3694 CB PRO 483 67.542 8.200 −0.947 1.00 47.02 ATOM 3695 CG PRO 483 67.269 7.666 −2.307 1.00 46.65 ATOM 3696 C PRO 483 66.991 6.151 0.429 1.00 48.74 ATOM 3697 O PRO 483 66.314 5.376 −0.251 1.00 48.01 ATOM 3698 N LEU 484 66.858 6.268 1.742 1.00 49.91 ATOM 3700 CA LEU 484 65.837 5.547 2.477 1.00 53.93 ATOM 3701 CB LEU 484 66.433 4.883 3.720 1.00 50.17 ATOM 3702 CG LEU 484 67.517 3.844 3.445 1.00 48.93 ATOM 3703 CD1 LEU 484 68.226 3.460 4.731 1.00 49.05 ATOM 3704 CD2 LEU 484 66.906 2.630 2.784 1.00 47.03 ATOM 3705 C LEU 484 64.715 6.501 2.878 1.00 58.70 ATOM 3706 O LEU 484 63.571 6.075 3.055 1.00 61.95 ATOM 3707 N GLY 485 66.027 7.788 3.006 1.00 60.35 ATOM 3709 CA GLY 485 63.998 8.737 3.397 1.00 64.00 ATOM 3710 C GLY 485 64.445 10.183 3.476 1.00 66.09 ATOM 3711 O GLY 485 65.643 10.468 3.577 1.00 65.26 ATOM 3712 N GLU 486 63.471 11.090 3.458 1.00 67.18 ATOM 3714 CA GLU 486 63.733 12.525 3.508 1.00 68.69 ATOM 3715 CB GLU 486 63.873 13.084 2.091 1.00 69.88 ATOM 3716 C GLU 486 62.618 13.249 4.245 1.00 68.80 ATOM 3717 O GLU 486 61.481 12.775 4.295 1.00 69.26 ATOM 3718 N GLY 487 62.943 14.415 4.791 1.00 68.47 ATOM 3720 CA GLY 487 61.960 15.188 5.520 1.00 67.56 ATOM 3721 C GLY 487 62.373 16.635 5.634 1.00 66.71 ATOM 3722 O GLY 487 63.040 17.172 4.747 1.00 66.48 ATOM 3723 N ALA 488 61.979 17.265 6.735 1.00 67.22 ATOM 3725 CA ALA 488 62.304 18.661 6.992 1.00 67.78 ATOM 3726 CB ALA 488 62.637 19.121 8.283 1.00 68.97 ATOM 3727 C ALA 488 63.817 18.830 7.085 1.00 67.38 ATOM 3728 O ALA 488 64.413 18.597 8.141 1.00 67.14 ATOM 3729 N PHE 489 64.429 19.155 5.946 1.00 66.22 ATOM 3731 CA PHE 489 65.877 19.364 5.831 1.00 65.49 ATOM 3732 CB PHE 489 66.277 20.699 6.467 1.00 66.11 ATOM 3733 C PHE 489 66.749 18.207 6.368 1.00 64.07 ATOM 3734 O PHE 489 67.924 18.399 6.731 1.00 61.56 ATOM 3735 N GLY 490 66.171 17.005 6.349 1.00 60.79 ATOM 3737 CA GLY 490 66.852 15.803 6.797 1.00 54.72 ATOM 3738 C GLY 490 66.787 14.760 5.692 1.00 51.78 ATOM 3739 O GLY 490 65.765 14.624 5.013 1.00 49.17 ATOM 3740 N GLN 491 67.874 14.015 5.528 1.00 49.97 ATOM 3742 CA GLN 491 68.000 12.984 4.504 1.00 48.06 ATOM 3743 CB GLN 491 68.891 13.520 3.371 1.00 51.02 ATOM 3744 CG GLN 491 69.286 12.518 2.289 1.00 56.00 ATOM 3745 CD GLN 491 70.155 13.143 1.202 1.00 58.93 ATOM 3746 OE1 GLN 491 70.483 14.330 1.255 1.00 60.31 ATOM 3747 NE2 GLN 491 70.529 12.341 0.202 1.00 60.19 ATOM 3750 C GLN 491 68.623 11.720 5.114 1.00 45.59 ATOM 3751 O GLN 491 69.511 11.792 5.959 1.00 45.22 ATOM 3752 N VAL 492 68.148 10.561 4.693 1.00 43.19 ATOM 3754 CA VAL 492 68.676 9.304 5.193 1.00 41.54 ATOM 3755 CB VAL 492 67.655 8.584 6.087 1.00 41.74 ATOM 3756 CG1 VAL 492 68.217 7.248 6.561 1.00 43.70 ATOM 3757 CG2 VAL 492 67.283 9.463 7.269 1.00 44.07 ATOM 3758 C VAL 492 68.971 8.424 3.993 1.00 39.72 ATOM 3759 O VAL 492 68.125 8.271 3.108 1.00 39.81 ATOM 3760 N VAL 493 70.176 7.872 3.942 1.00 36.38 ATOM 3762 CA VAL 493 70.545 7.001 2.844 1.00 35.88 ATOM 3763 CB VAL 493 71.580 7.666 1.869 1.00 36.92 ATOM 3764 CG1 VAL 493 71.142 9.069 1.485 1.00 36.64 ATOM 3765 CG2 VAL 493 72.978 7.670 2.469 1.00 38.29 ATOM 3766 C VAL 493 71.131 5.689 3.351 1.00 36.03 ATOM 3767 O VAL 493 71.693 5.617 4.443 1.00 36.57 ATOM 3768 N LEU 494 70.947 4.637 2.571 1.00 34.91 ATOM 3770 CA LEU 494 71.500 3.344 2.909 1.00 36.04 ATOM 3771 CB LEU 494 70.809 2.244 2.094 1.00 37.43 ATOM 3772 CG LEU 494 71.312 0.814 2.269 1.00 36.62 ATOM 3773 CD1 LEU 494 71.327 0.437 3.735 1.00 36.37 ATOM 3774 CD2 LEU 494 70.419 −0.118 1.479 1.00 40.70 ATOM 3775 C LEU 494 72.967 3.451 2.510 1.00 37.08 ATOM 3776 O LEU 494 73.308 4.160 1.560 1.00 34.90 ATOM 3777 N ALA 495 73.839 2.779 3.243 1.00 37.18 ATOM 3779 CA ALA 495 75.246 2.830 2.918 1.00 39.84 ATOM 3780 CB ALA 495 75.885 4.066 3.541 1.00 39.29 ATOM 3781 C ALA 495 75.949 1.578 3.400 1.00 41.68 ATOM 3782 O ALA 495 75.400 0.808 4.189 1.00 41.53 ATOM 3783 N GLU 496 77.149 1.348 2.881 1.00 43.44 ATOM 3785 CA GLU 496 77.936 0.202 3.297 1.00 42.86 ATOM 3786 CB GLU 496 78.328 −0.663 2.101 1.00 44.63 ATOM 3787 CG GLU 496 77.120 −2.167 1.320 1.00 53.31 ATOM 3788 CD GLU 496 77.386 −2.450 0.545 1.00 59.48 ATOM 3789 OE1 GLU 496 76.494 −3.332 0.534 1.00 62.39 ATOM 3790 OE2 GLU 496 78.477 −2.580 −0.053 1.00 62.15 ATOM 3791 C GLU 496 79.150 0.750 4.006 1.00 40.96 ATOM 3792 O GLU 496 79.889 1.568 3.455 1.00 40.81 ATOM 3793 N ALA 497 79.267 0.411 5.280 1.00 40.79 ATOM 3795 CA ALA 497 80.381 0.857 6.096 1.00 41.84 ATOM 3796 CB ALA 497 79.888 1.240 7.478 1.00 38.80 ATOM 3797 C ALA 497 81.394 −0.280 6.181 1.00 44.72 ATOM 3798 O ALA 497 81.019 −1.445 6.215 1.00 44.78 ATOM 3799 N ILE 498 82.678 0.054 6.183 1.00 48.03 ATOM 3801 CA ILE 498 83.729 −0.952 6.255 1.00 48.78 ATOM 3802 CB ILE 498 84.654 −0.894 5.014 1.00 50.57 ATOM 3803 CG2 ILE 498 85.748 −1.954 5.119 1.00 51.32 ATOM 3804 CG1 ILE 498 83.851 −1.103 3.726 1.00 51.90 ATOM 3805 CD1 ILE 498 83.139 0.146 3.198 1.00 55.47 ATOM 3806 C ILE 498 84.573 −0.754 7.511 1.00 48.31 ATOM 3807 O ILE 498 85.005 0.359 7.805 1.00 47.90 ATOM 3808 N GLY 499 84.754 −1.829 8.271 1.00 49.29 ATOM 3810 CA GLY 499 85.563 −1.774 9.479 1.00 53.17 ATOM 3811 C GLY 499 85.076 −0.944 10.657 1.00 57.22 ATOM 3812 O GLY 499 85.885 −0.341 11.364 1.00 59.20 ATOM 3813 N LEU 500 83.768 −0.948 10.909 1.00 58.51 ATOM 3815 CA LEU 500 83.193 −0.189 12.023 1.00 57.80 ATOM 3816 CB LEU 500 81.705 −0.519 12.181 1.00 55.67 ATOM 3817 CG LEU 500 80.789 0.036 11.086 1.00 54.81 ATOM 3818 CD1 LEU 500 79.361 −0.445 11.293 1.00 53.00 ATOM 3819 CD2 LEU 500 80.854 1.561 11.089 1.00 53.27 ATOM 3820 C LEU 500 83.926 −0.466 13.333 1.00 58.15 ATOM 3821 O LEU 500 84.461 −1.560 13.529 1.00 60.29 ATOM 3822 N PRO 505 87.397 −6.022 10.511 1.00 77.18 ATOM 3823 CD PRO 505 88.509 −6.651 11.242 1.00 78.26 ATOM 3824 CA PRO 505 87.755 −4.660 10.097 1.00 75.62 ATOM 3825 CB PRO 505 89.166 −4.487 10.669 1.00 75.77 ATOM 3826 CG PRO 505 89.696 −5.884 10.715 1.00 77.07 ATOM 3827 C PRO 505 87.709 −4.440 8.583 1.00 73.15 ATOM 3828 O PRO 505 87.772 −3.308 8.105 1.00 72.63 ATOM 3829 N ASN 506 87.595 −5.524 7.830 1.00 71.27 ATOM 3831 CA ASN 506 87.518 −5.421 6.380 1.00 69.14 ATOM 3832 CB ASN 506 88.577 −6.313 5.728 1.00 70.76 ATOM 3833 C ASN 506 86.119 −5.840 5.940 1.00 67.30 ATOM 3834 O ASN 506 85.834 −5.957 4.750 1.00 67.03 ATOM 3835 N ARG 507 85.250 −6.064 6.921 1.00 65.27 ATOM 3837 CA ARG 507 83.876 −6.479 6.669 1.00 62.86 ATOM 3838 CB ARG 507 83.335 −7.267 7.864 1.00 65.45 ATOM 3839 C ARG 507 82.991 −5.274 6.443 1.00 59.56 ATOM 3840 O ARG 507 83.161 −4.247 7.100 1.00 59.70 ATOM 3841 N VAL 508 82.057 −5.397 5.509 1.00 56.65 ATOM 3843 CA VAL 508 81.135 −4.310 5.226 1.00 55.48 ATOM 3844 CB VAL 508 80.850 −4.157 3.719 1.00 55.71 ATOM 3845 CG1 VAL 508 82.146 −3.962 2.962 1.00 58.18 ATOM 3846 CG2 VAL 508 80.096 −5.356 3.188 1.00 58.76 ATOM 3847 C VAL 508 79.833 −4.537 5.979 1.00 53.10 ATOM 3848 O VAL 508 79.352 −5.665 6.091 1.00 54.25 ATOM 3849 N THR 509 79.282 −3.460 6.514 1.00 50.06 ATOM 3851 CA THR 509 78.041 −3.512 7.260 1.00 45.70 ATOM 3852 CB THR 509 78.256 −3.029 8.715 1.00 45.59 ATOM 3853 OG1 THR 509 79.395 −3.696 9.279 1.00 43.86 ATOM 3855 CG2 THR 509 77.028 −3.328 9.573 1.00 44.19 ATOM 3856 C THR 509 77.064 −2.574 6.564 1.00 43.57 ATOM 3857 O THR 509 77.416 −1.444 6.221 1.00 41.15 ATOM 3858 N LYS 510 75.871 −3.073 6.268 1.00 42.96 ATOM 3860 CA LYS 510 74.847 −2.253 3.640 1.00 41.91 ATOM 3861 CS LYS 510 73.740 −3.144 5.091 1.00 44.74 ATOM 3862 CG LYS 510 72.864 −2.461 4.069 1.00 51.83 ATOM 3863 CD LYS 510 73.392 −2.645 2.659 1.00 55.00 ATOM 3864 CE LYS 510 72.769 −3.879 2.020 1.00 58.36 ATOM 3865 NZ LYS 510 73.069 −5.131 2.769 1.00 58.57 ATOM 3869 C LYS 510 74.322 −1.367 6.789 1.00 40.74 ATOM 3870 O LYS 510 73.909 −1.874 7.837 1.00 40.26 ATOM 3871 N VAL 511 74.413 −0.052 6.624 1.00 37.21 ATOM 3873 CA VAL 511 73.989 0.877 7.661 1.00 33.44 ATOM 3874 CB VAL 511 75.227 1.515 8.362 1.00 34.53 ATOM 3875 CG1 VAL 511 76.100 0.436 9.014 1.00 31.98 ATOM 3876 CG2 VAL 511 76.048 2.322 7.358 1.00 34.82 ATOM 3877 C VAL 511 73.134 1.989 7.087 1.00 31.34 ATOM 3878 O VAL 511 73.025 2.130 5.871 1.00 31.33 ATOM 3879 N ALA 512 72.485 2.748 7.961 1.00 30.70 ATOM 3881 CA ALA 512 71.671 3.876 7.523 1.00 30.81 ATOM 3882 CB ALA 512 70.305 3.879 8.206 1.00 29.85 ATOM 3883 C ALA 512 72.453 5.124 7.904 1.00 31.30 ATOM 3884 O ALA 512 73.036 5.197 8.996 1.00 30.24 ATOM 3885 N VAL 513 72.480 5.096 6.999 1.00 30.86 ATOM 3887 CA VAL 513 73.208 7.332 7.238 1.00 30.58 ATOM 3888 CB VAL 513 74.358 7.525 6.223 1.00 31.11 ATOM 3889 CG1 VAL 513 75.132 8.788 6.547 1.00 29.63 ATOM 3890 CG2 VAL 513 75.290 6.317 6.223 1.00 28.70 ATOM 3892 C VAL 513 72.300 8.556 7.189 1.00 31.28 ATOM 3892 O VAL 513 71.645 8.824 6.167 1.00 30.12 ATOM 3893 N LYS 514 72.229 9.257 8.321 1.00 31.03 ATOM 3895 CA LYS 514 71.439 10.479 8.451 1.00 32.56 ATOM 3896 CB LYS 514 70.881 10.635 9.870 1.00 34.31 ATOM 3897 CG LYS 514 69.977 9.516 10.326 1.00 38.25 ATOM 3898 CD LYS 514 69.513 9.774 11.753 1.00 47.74 ATOM 3899 CE LYS 514 68.514 8.719 12.230 1.00 51.60 ATOM 3900 NZ LYS 514 67.226 8.755 11.468 1.00 58.53 ATOM 3904 C LYS 514 72.357 11.659 8.137 1.00 30.29 ATOM 3905 O LYS 514 73.485 11.736 8.628 1.00 28.14 ATOM 3906 N MET 515 71.867 12.580 7.320 1.00 30.67 ATOM 3908 CA MET 515 72.643 13.747 6.920 1.00 29.94 ATOM 3909 CB MET 515 73.435 13.442 5.648 1.00 30.64 ATOM 3910 CG MET 515 72.557 13.038 4.464 1.00 32.16 ATOM 3911 SD MET 515 73.525 12.522 3.036 1.00 37.59 ATOM 3912 CE MET 515 74.015 10.933 3.563 1.00 29.11 ATOM 3913 C MET 515 71.675 14.869 6.635 1.00 29.71 ATOM 3914 O MET 515 70.462 14.664 6.598 1.00 30.04 ATOM 3915 N LEU 516 72.212 16.060 6.445 1.00 29.56 ATOM 3917 CA LEU 516 71.381 17.206 6.136 1.00 30.76 ATOM 3918 CB LEU 516 72.093 18.508 6.526 1.00 28.20 ATOM 3919 CG LEU 516 72.396 18.724 8.011 1.00 28.48 ATOM 3920 CD1 LEU 516 73.202 19.983 8.185 1.00 27.55 ATOM 3921 CD2 LEU 516 71.114 18.814 8.794 1.00 25.49 ATOM 3922 C LEU 516 71.081 17.225 4.647 1.00 30.97 ATOM 3923 O LEU 516 71.728 16.534 3.851 1.00 29.93 ATOM 3924 N LYS 517 70.030 17.946 4.291 1.00 31.57 ATOM 3926 CA LYS 517 69.677 18.117 2.899 1.00 31.44 ATOM 3927 CB LYS 517 68.169 18.310 2.752 1.00 34.79 ATOM 3928 CG LYS 517 67.375 17.098 3.194 1.00 38.42 ATOM 3929 CD LYS 517 66.148 16.888 2.343 1.00 46.52 ATOM 3930 CE LYS 517 65.087 17.950 2.582 1.00 53.77 ATOM 3931 NZ LYS 517 63.901 17.740 1.690 1.00 56.38 ATOM 3935 C LYS 517 70.457 19.377 2.499 1.00 30.18 ATOM 3936 O LYS 517 70.892 20.134 3.370 1.00 27.47 ATOM 3937 N SER 518 70.646 19.594 1.201 1.00 31.13 ATOM 3539 CA SER 518 71.394 20.747 0.693 1.00 32.11 ATOM 3940 CB SER 518 71.518 20.652 −0.824 1.00 33.45 ATOM 3941 OG SER 518 70.242 20.567 −1.428 1.00 34.51 ATOM 3943 C SER 518 70.814 22.103 1.073 1.00 32.81 ATOM 3944 O SER 518 71.515 23.123 1.027 1.00 34.03 ATOM 3945 N ASP 519 69.540 22.117 1.449 1.00 29.80 ATOM 3947 CA ASP 519 68.886 23.354 1.836 1.00 28.94 ATOM 3948 CB ASP 519 67.473 23.421 1.237 1.00 33.90 ATOM 3949 CG ASP 519 66.542 22.332 1.771 1.00 34.42 ATOM 3950 OD1 ASP 519 67.020 21.328 2.333 1.00 35.58 ATOM 3951 OD2 ASP 519 65.313 22.485 1.617 1.00 41.83 ATOM 3952 C ASP 519 68.829 23.559 3.342 1.00 29.08 ATOM 3953 O ASP 519 68.177 24.485 3.816 1.00 29.79 ATOM 3954 N ALA 520 69.514 22.710 4.099 1.00 29.73 ATOM 3956 CA ALA 520 69.488 22.824 5.558 1.00 29.16 ATOM 3957 CB ALA 520 70.174 21.639 6.190 1.00 28.13 ATOM 3958 C ALA 520 70.122 24.108 6.040 1.00 28.06 ATOM 3959 O ALA 520 70.880 24.741 5.309 1.00 28.84 ATOM 3960 N THR 521 69.800 24.491 7.272 1.00 27.84 ATOM 3962 CA THR 521 70.357 25.692 7.885 1.00 30.45 ATOM 3963 CB THR 521 69.254 26.635 8.463 1.00 33.56 ATOM 3964 OG1 THR 521 68.547 25.968 9.520 1.00 36.27 ATOM 3966 CG2 THR 521 68.275 27.074 7.379 1.00 36.06 ATOM 3967 C THR 522 71.251 25.263 9.048 1.00 30.04 ATOM 3968 O THR 521 71.348 24.072 9.369 1.00 28.16 ATOM 3969 N GLU 522 72.876 26.241 9.696 1.00 31.42 ATOM 3971 CA GLU 522 72.745 25.978 10.832 1.00 36.94 ATOM 3972 CB GLU 522 73.404 27.282 11.299 1.00 44.74 ATOM 3973 CG GLU 522 74.414 27.130 12.450 1.00 58.34 ATOM 3974 CD GLU 522 75.769 26.579 12.009 1.00 64.50 ATOM 3975 OE1 GLU 522 76.798 27.261 12.231 1.00 64.89 ATOM 3976 OE2 GLU 522 75.806 25.461 11.452 1.00 70.26 ATOM 3977 C GLU 522 71.932 25.345 11.969 1.00 34.02 ATOM 3978 O GLU 522 72.428 24.480 12.684 1.00 31.11 ATOM 3979 N LYS 523 70.670 25.750 12.097 1.00 32.53 ATOM 3981 CA LYS 523 69.805 25.210 13.135 1.00 34.06 ATOM 3982 CB LYS 523 68.481 25.970 13.188 1.00 39.54 ATOM 3983 CG LYS 523 67.560 25.541 14.322 1.00 45.55 ATOM 3984 CD LYS 523 66.360 24.776 13.789 1.00 52.08 ATOM 3985 CE LYS 523 65.443 24.312 14.914 1.00 54.16 ATOM 3986 NZ LYS 523 64.313 23.509 14.373 1.00 54.38 ATOM 3990 C LYS 523 69.572 23.733 12.861 1.00 31.73 ATOM 3991 O LYS 523 69.589 22.922 13.788 1.00 31.15 ATOM 3992 N ASP 524 69.374 23.383 11.590 1.00 29.22 ATOM 3994 CA ASP 524 69.182 21.980 11.214 1.00 28.79 ATOM 3995 CB ASP 524 68.928 21.831 9.714 1.00 27.65 ATOM 3996 CG ASP 524 67.586 22.396 9.286 1.00 33.89 ATOM 3997 OD1 ASP 524 66.568 22.106 9.954 1.00 34.66 ATOM 3998 OD2 ASP 524 67.549 23.120 8.270 1.00 30.04 ATOM 3999 C ASP 524 70.424 21.190 11.606 1.00 28.00 ATOM 4000 O ASP 524 70.317 20.104 12.162 1.00 30.83 ATOM 4001 N LEU 525 71.603 21.761 11.347 1.00 29.87 ATOM 4003 CA LEU 525 72.873 21.121 11.700 1.00 27.60 ATOM 4004 CB LEU 525 74.064 21.997 11.282 1.00 24.08 ATOM 4005 CG LEU 525 75.462 21.433 11.593 1.00 26.11 ATOM 4006 CD1 LEU 525 75.597 19.979 11.098 1.00 23.67 ATOM 4007 CD2 LEU 525 76.530 22.321 10.967 1.00 21.28 ATOM 4008 C LEU 525 72.909 20.869 13.200 1.00 26.38 ATOM 4009 O LEU 525 73.249 19.777 13.553 1.00 26.09 ATOM 4010 N SER 526 72.560 21.902 13.956 1.00 29.72 ATOM 4012 CA SER 526 72.500 21.861 15.422 1.00 32.16 ATOM 4013 CB SER 526 71.980 23.209 15.939 1.00 33.45 ATOM 4014 OG SER 526 71.793 23.213 17.343 1.00 40.42 ATOM 4016 C SER 526 71.572 20.728 15.902 1.00 31.64 ATOM 4017 O SER 526 71.869 20.030 16.889 1.00 32.54 ATOM 4018 N ASP 527 70.454 20.561 15.201 1.00 27.92 ATOM 4020 CA ASP 527 69.492 19.527 15.524 1.00 28.60 ATOM 4021 CB ASP 527 68.187 19.767 14.765 1.00 29.35 ATOM 4022 CG ASP 527 67.418 20.984 15.278 1.00 31.37 ATOM 4023 OD1 ASP 527 67.759 21.549 16.353 1.00 31.96 ATOM 4024 OD2 ASP 527 66.456 21.369 14.591 1.00 32.58 ATOM 4025 C ASP 527 70.038 18.131 15.246 1.00 28.82 ATOM 4026 O ASP 527 69.854 17.212 16.047 1.00 29.65 ATOM 4027 N LEU 528 70.721 17.962 14.120 1.00 29.29 ATOM 4029 CA LEU 528 71.302 16.658 13.794 1.00 29.94 ATOM 4030 CB LEU 528 71.780 16.621 12.336 1.00 26.45 ATOM 4031 CG LEU 528 72.315 15.276 11.840 1.00 28.34 ATOM 4032 CD1 LEU 528 71.240 14.189 12.035 1.00 27.16 ATOM 4033 CD2 LEU 528 72.756 15.387 10.372 1.00 25.91 ATOM 4034 C LEU 528 72.449 16.319 14.776 1.00 29.72 ATOM 4035 O LEU 528 72.617 15.162 15.178 1.00 28.98 ATOM 4036 N ILE 529 73.224 17.329 15.168 1.00 30.15 ATOM 4038 CA ILE 529 74.305 17.131 16.134 1.00 28.88 ATOM 4039 CB ILE 529 75.188 18.382 16.268 1.00 26.91 ATOM 4040 CG2 ILE 529 76.175 18.221 17.423 1.00 24.82 ATOM 4041 CG1 ILE 529 75.960 18.613 14.984 1.00 23.98 ATOM 4042 CD1 ILE 529 76.663 19.932 14.973 1.00 28.33 ATOM 4043 C ILE 529 73.709 16.799 17.518 1.00 29.71 ATOM 4044 O ILE 529 74.172 15.880 18.193 1.00 29.19 ATOM 4045 N SER 530 72.672 17.524 17.926 1.00 26.84 ATOM 4047 CA SER 530 72.061 17.247 19.214 1.00 31.46 ATOM 4048 CB SER 530 70.948 18.251 19.521 1.00 36.17 ATOM 4049 OG SER 530 70.045 18.363 18.431 1.00 47.58 ATOM 4051 C SER 530 71.526 15.822 19.248 1.00 30.05 ATOM 4052 O SER 530 71.646 15.136 20.270 1.00 29.61 ATOM 4053 N GLU 531 70.972 15.357 18.132 1.00 27.74 ATOM 4055 CA GLU 531 70.458 13.999 18.090 1.00 28.71 ATOM 4056 CB GLU 531 69.709 13.727 16.789 1.00 29.72 ATOM 4057 CG GLU 531 69.147 12.319 16.737 1.00 32.21 ATOM 4058 CD GLU 531 68.510 11.979 15.414 1.00 33.88 ATOM 4059 0E1 GLU 531 68.026 10.846 15.281 1.00 37.60 ATOM 4060 0E2 GLU 531 68.483 12.833 14.510 1.00 34.70 ATOM 4061 C GLU 531 71.578 12.974 18.271 1.00 28.91 ATOM 4062 O GLU 531 71.428 12.007 19.019 1.00 29.46 ATOM 4063 N MET 532 72.686 13.179 17.567 1.00 28.84 ATOM 4065 CA MET 532 73.851 12.296 17.648 1.00 29.35 ATOM 4066 CB MET 532 74.948 12.786 16.689 1.00 27.41 ATOM 4067 CG MET 532 76.299 12.117 16.872 1.00 26.71 ATOM 4068 SD MET 532 77.503 12.675 15.640 1.00 32.27 ATOM 4069 CE MET 532 77.732 14.400 16.117 1.00 24.10 ATOM 4070 C MET 532 74.389 12.280 19.078 1.00 28.80 ATOM 4071 O MET 532 74.700 11.230 19.630 1.00 29.74 ATOM 4072 N GLU 533 74.481 13.454 19.681 1.00 28.83 ATOM 4074 CA GLU 533 74.985 13.546 21.033 1.00 29.66 ATOM 4075 CB GLU 533 75.182 15.008 21.423 1.00 32.23 ATOM 4076 CG GLU 533 76.331 15.687 20.651 1.00 34.47 ATOM 4077 CD GLU 533 77.656 14.937 20.774 1.00 38.03 ATOM 4078 OE1 GLU 533 78.168 14.780 21.903 1.00 39.75 ATOM 4079 OE2 GLU 533 78.192 14.497 19.736 1.00 38.75 ATOM 4080 C GLU 533 74.058 12.815 22.005 1.00 31.55 ATOM 4081 O GLU 533 74.521 12.083 22.889 1.00 30.63 ATOM 4082 N MET 534 72.750 12.958 21.799 1.00 31.31 ATOM 4084 CA MET 534 71.789 12.289 22.664 1.00 30.78 ATOM 4085 CB MET 534 70.348 12.672 22.319 1.00 31.23 ATOM 4086 CG MET 534 69.453 12.648 23.551 0.50 29.35 PRT1 ATOM 4087 SD MET 534 67.688 12.563 23.246 0.50 28.79 PRT1 ATOM 4088 CE MET 534 67.290 14.230 22.875 0.50 26.96 PRT1 ATOM 4089 C MET 534 71.991 10.773 22.560 1.00 28.82 ATOM 4090 O MET 534 72.053 10.083 23.568 1.00 30.10 ATOM 4091 N MET 535 72.149 10.271 21.339 1.00 29.16 ATOM 4093 CA MET 535 72.381 8.852 21.110 1.00 29.37 ATOM 4094 CB MET 535 72.546 8.551 19.617 1.00 27.35 ATOM 4095 CG MET 535 71.281 8.790 18.817 1.00 28.40 ATOM 4096 SD MET 535 71.255 7.955 17.255 1.00 30.26 ATOM 4097 CE MET 535 71.336 9.279 16.188 1.00 35.50 ATOM 4098 C MET 535 73.612 8.388 21.887 1.00 30.36 ATOM 4099 O MET 535 73.626 7.287 22.460 1.00 26.13 ATOM 4100 N LYS 536 74.640 9.233 21.909 1.00 30.70 ATOM 4102 CA LYS 536 75.850 8.913 22.649 1.00 31.16 ATOM 4103 CB LYS 536 76.934 9.954 22.388 1.00 31.05 ATOM 4104 OG LYS 536 77.550 9.883 21.004 1.00 26.80 ATOM 4105 CD LYS 536 78.534 11.017 20.860 1.00 31.05 ATOM 4106 CE LYS 536 79.132 11.138 19.466 1.00 29.83 ATOM 4107 NZ LYS 536 79.957 12.377 19.440 1.00 29.32 ATOM 4111 C LYS 536 75.550 8.834 24.150 1.00 31.99 ATOM 4112 O LYS 536 75.920 7.859 24.806 1.00 31.92 ATOM 4113 N MET 537 74.837 9.826 24.676 1.00 31.81 ATOM 4115 CA MET 537 74.517 9.835 26.090 1.00 35.37 ATOM 4116 CB MET 537 73.860 11.154 26.506 1.00 41.32 ATOM 4117 CG MET 537 74.828 12.335 26.610 1.00 51.50 ATOM 4118 SD MET 537 76.234 12.090 27.776 1.00 57.48 ATOM 4119 CE MET 537 75.460 12.637 29.334 1.00 56.91 ATOM 4120 C MET 537 73.630 8.679 26.499 1.00 36.11 ATOM 4121 O MET 537 73.845 8.084 27.548 1.00 38.54 ATOM 4122 N IIE 538 72.652 8.347 25.661 1.00 33.69 ATOM 4124 CA ILE 538 71.704 7.277 25.954 1.00 31.62 ATOM 4125 CB ILE 538 70.492 7.314 24.974 1.00 28.21 ATOM 4126 CG2 ILE 538 69.681 6.013 25.034 1.00 28.22 ATOM 4127 CG1 ILE 538 69.590 8.488 25.338 1.00 23.74 ATOM 4128 CD1 ILE 538 68.487 8.728 24.344 1.00 27.94 ATOM 4129 C ILE 538 72.322 5.894 26.008 1.00 31.07 ATOM 4130 O ILE 538 71.952 5.080 26.860 1.00 33.13 ATOM 4131 N GLY 539 73.239 5.611 25.094 1.00 29.52 ATOM 4133 CA GLY 539 73.871 4.309 25.093 1.00 28.40 ATOM 4134 C GLY 539 73.111 3.275 24.289 1.00 30.21 ATOM 4135 O GLY 539 72.018 3.554 23.788 1.00 29.66 ATOM 4136 N LYS 540 73.679 2.074 24.199 1.00 28.44 ATOM 4138 CA LYS 540 73.105 0.984 23.426 1.00 31.09 ATOM 4139 CB LYS 540 74.215 0.089 22.895 1.00 33.15 ATOM 4140 CH LYS 540 75.116 0.776 21.906 1.00 39.54 ATOM 4141 CD LYS 540 76.125 −0.175 21.329 1.00 43.98 ATOM 4142 CE LYS 540 77.033 0.562 20.349 1.00 50.79 ATOM 4143 NZ LYS 540 76.338 0.977 19.086 1.00 51.09 ATOM 4147 C LYS 540 72.053 0.087 24.059 1.00 32.78 ATOM 4148 O LYS 540 72.088 −0.195 25.266 1.00 32.41 ATOM 4149 N HIS 541 71.137 −0.374 23.208 1.00 31.20 ATOM 4151 CA HIS 541 70.080 −1.304 23.591 1.00 31.53 ATOM 4152 CB HIS 541 68.911 −0.630 24.298 1.00 30.69 ATOM 4153 CG HIS 541 67.948 −1.613 24.882 1.00 31.18 ATOM 4154 CD2 HIS 541 67.938 −2.255 26.072 1.00 33.02 ATOM 4155 ND1 HIS 541 66.882 −2.123 24.165 1.00 30.56 ATOM 4157 CE1 HIS 541 66.268 −3.037 24.889 1.00 32.95 ATOM 4158 NE2 HIS 541 66.886 −3.140 26.053 1.00 31.79 ATOM 4160 C HIS 541 69.590 −2.013 22.340 1.00 32.72 ATOM 4161 O HIS 541 69.495 −1.404 21.275 1.00 30.34 ATOM 4162 N LYS 542 69.282 −3.305 22.475 1.00 32.32 ATOM 4164 CA LYS 542 68.828 −4.131 21.359 1.00 30.29 ATOM 4165 CB LYS 542 68.637 −5.587 21.798 1.00 29.34 ATOM 4166 C LYS 542 67.560 −3.661 20.692 1.00 29.09 ATOM 4167 O LYS 542 67.369 −3.903 19.507 1.00 29.12 ATOM 4168 N ASN 543 66.683 −3.012 21.446 1.00 28.54 ATOM 4170 CA ASN 543 65.425 −2.559 20.869 1.00 29.10 ATOM 4171 CB ASN 543 64.245 −3.047 21.712 1.00 29.69 ATOM 4172 CG ASN 543 64.253 −4.556 21.900 1.00 29.62 ATOM 4173 OD1 ASN 543 64.510 −5.050 23.000 1.00 31.63 ATOM 4174 ND2 ASN 543 64.020 −5.291 20.828 1.00 28.66 ATOM 4177 C ASN 543 65.299 −1.073 20.532 1.00 29.61 ATOM 4178 O ASN 543 64.207 −0.507 20.578 1.00 28.00 ATOM 4179 N ILE 544 66.432 −0.442 20.222 1.00 28.39 ATOM 4181 CA ILE 544 66.466 0.958 19.804 1.00 25.73 ATOM 4182 CB ILE 544 66.903 1.952 20.935 1.00 25.98 ATOM 4183 CG2 ILE 544 66.083 1.721 22.215 1.00 22.04 ATOM 4184 CG1 ILE 544 68.412 1.860 21.209 1.00 24.30 ATOM 4185 CD1 ILE 544 68.901 2.846 22.274 1.00 22.83 ATOM 4186 C ILE 544 67.463 1.020 18.639 1.00 26.20 ATOM 4187 O ILE 544 68.276 0.106 18.467 1.00 25.46 ATOM 4188 N ILE 545 67.307 2.016 17.771 1.00 26.26 ATOM 4190 CA ILE 545 68.223 2.209 16.641 1.00 27.62 ATOM 4191 CB ILE 545 67.647 3.195 15.585 1.00 28.33 ATOM 4192 CG2 ILE 545 68.726 3.595 14.562 1.00 28.00 ATOM 4193 CG1 ILE 545 66.453 2.565 14.856 1.00 24.69 ATOM 4194 CD1 ILE 545 66.850 1.467 13.875 1.00 26.17 ATOM 4195 C ILE 545 69.492 2.794 17.267 1.00 28.23 ATOM 4196 O ILE 545 69.468 3.872 17.846 1.00 28.97 ATOM 4397 N ASN 546 70.595 2.069 17.164 1.00 29.45 ATOM 4199 CA ASN 546 71.845 2.508 17.774 1.00 28.58 ATOM 4200 CB ASN 546 72.580 1.309 18.384 1.00 26.34 ATOM 4201 CG ASN 546 71.812 0.673 19.527 1.00 25.52 ATOM 4202 OD1 ASN 546 71.634 1.277 20.580 1.00 28.82 ATOM 4203 ND2 ASN 546 71.341 −0.542 19.318 1.00 26.57 ATOM 4206 C ASN 546 72.810 3.264 16.881 1.00 28.74 ATOM 4207 O ASN 546 72.858 3.041 15.675 1.00 29.26 ATOM 4208 N LEU 547 73.578 4.155 17.504 1.00 29.90 ATOM 4210 CA LEU 547 74.618 4.936 16.834 1.00 30.27 ATOM 4211 CB LEU 547 75.075 6.081 17.745 1.00 25.85 ATOM 4212 CG LEU 547 76.161 1.034 17.232 1.00 27.73 ATOM 4213 CD1 LEU 547 75.670 7.851 16.033 1.00 27.38 ATOM 4214 CD2 LEU 547 76.545 7.966 18.345 1.00 29.34 ATOM 4215 C LEU 547 75.811 4.004 16.567 1.00 32.22 ATOM 4216 O LEU 547 76.256 3.291 17.471 1.00 33.38 ATOM 4217 N LEU 548 76.317 4.005 15.335 1.00 32.12 ATOM 4219 CA LEU 548 77.452 3.159 14.960 1.00 32.94 ATOM 4220 CB LEU 548 77.103 2.310 13.740 1.00 29.97 ATOM 4221 CG LEU 548 75.839 1.458 13.840 1.00 31.55 ATOM 4222 CD1 LEU 548 75.662 0.713 12.540 1.00 27.85 ATOM 4223 CD2 LEU 548 75.917 0.500 15.025 1.00 26.34 ATOM 4224 C LEU 548 78.726 3.955 14.654 1.00 36.06 ATOM 4225 O LEU 548 79.836 3.410 14.668 1.00 36.42 ATOM 4226 N GLY 549 78.562 5.219 14.298 1.00 35.78 ATOM 4228 CA GLY 549 79.713 6.042 13.987 1.00 36.22 ATOM 4229 C GLY 549 79.267 7.376 13.433 1.00 35.30 ATOM 4230 O GLY 549 78.062 7.646 13.362 1.00 33.46 ATOM 4231 N ALA 550 80.232 8.206 13.042 1.00 34.94 ATOM 4233 CA ALA 550 79.945 9.525 12.490 1.00 31.91 ATOM 4234 CB ALA 550 79.588 10.495 13.613 1.00 30.54 ATOM 4235 C ALA 550 81.128 10.077 11.715 1.00 31.58 ATOM 4236 O ALA 550 82.281 9.832 12.080 1.00 31.23 ATOM 4237 N CYS 551 80.818 10.812 10.643 1.00 31.13 ATOM 4239 CA CYS 551 81.805 11.503 9.804 1.00 28.28 ATOM 4240 CB CYS 551 81.621 11.180 8.316 1.00 27.27 ATOM 4241 SG CYS 551 81.771 9.449 7.839 1.00 30.33 ATOM 4242 C CYS 551 81.450 12.960 10.074 1.00 25.88 ATOM 4243 O CYS 551 80.432 13.458 9.605 1.00 27.73 ATOM 4244 N THR 552 82.214 13.586 10.954 1.00 25.35 ATOM 4246 CA THR 552 81.988 14.967 11.353 1.00 26.79 ATOM 4247 CB THR 552 82.051 15.092 12.899 1.00 27.76 ATOM 4248 OG1 THR 552 83.392 14.839 13.338 1.00 27.62 ATOM 4250 CG2 THR 552 81.119 14.086 13.575 1.00 29.17 ATOM 4251 C THR 552 83.036 15.931 10.790 1.00 25.03 ATOM 4252 O THR 552 82.825 17.137 10.746 1.00 25.34 ATOM 4253 N GLN 553 84.174 15.385 10.381 1.00 27.34 ATOM 4255 CA GLN 553 85.285 16.190 9.888 1.00 26.31 ATOM 4256 CB GLN 553 86.601 15.639 10.468 1.00 25.05 ATOM 4257 CG GLN 553 86.581 15.491 11.993 1.00 24.78 ATOM 4258 CD GLN 553 86.382 16.823 12.709 1.00 25.40 ATOM 4259 OE1 GLN 553 87.175 17.748 12.546 1.00 33.74 ATOM 4260 NE2 GLN 553 85.338 16.920 13.516 1.00 25.61 ATOM 4263 C GLN 553 85.390 16.274 8.379 1.00 27.08 ATOM 4264 O GLN 553 85.083 15.318 7.669 1.00 28.76 ATOM 4265 N ASP 554 85.804 17.438 7.899 1.00 28.63 ATOM 4267 CA ASP 554 86.015 17.677 6.471 1.00 29.70 ATOM 4268 CB ASP 554 87.335 17.050 6.051 1.00 29.73 ATOM 4269 CG ASP 554 88.480 17.587 6.857 1.00 33.38 ATOM 4270 OD1 ASP 554 88.794 18.780 6.711 1.00 36.53 ATOM 4271 OD2 ASP 554 89.024 16.841 7.687 1.00 36.40 ATOM 4272 C ASP 554 84.908 17.258 5.522 1.00 29.64 ATOM 4273 O ASP 554 85.112 16.422 4.643 1.00 32.06 ATOM 4274 N GLY 555 83.748 17.881 5.679 1.00 28.59 ATOM 4276 CA GLY 555 82.620 17.573 4.825 1.00 26.85 ATOM 4277 C GLY 555 81.333 17.434 5.607 1.00 25.30 ATOM 4278 O GLY 555 81.319 17.593 6.834 1.00 23.96 ATOM 4279 N PRO 556 80.229 17.113 4.920 1.00 24.84 ATOM 4280 CD PRO 556 80.159 16.850 3.472 1.00 21.36 ATOM 4281 CA PRO 556 78.920 16.942 5.550 1.00 25.26 ATOM 4282 CB PRO 556 78.033 16.494 4.386 1.00 23.37 ATOM 4283 CG PRO 556 79.025 1S.881 3.398 1.00 24.44 ATOM 4284 C PRO 556 78.885 15.941 6.700 1.00 26.50 ATOM 4285 O PRO 556 79.515 14.875 6.654 1.00 27.38 ATOM 4286 N LEU 557 78.171 16.314 7.754 1.00 26.25 ATOM 4288 CA LEU 557 78.032 15.452 8.917 1.00 28.25 ATOM 4289 CB LEU 557 77.403 16.217 10.092 1.00 27.09 ATOM 4290 CG LEU 557 76.922 15.414 11.310 1.00 28.35 ATOM 4291 CD1 LEU 557 78.088 14.733 12.011 1.00 25.54 ATOM 4292 CD2 LEU 557 76.204 16.340 12.271 1.00 26.91 ATOM 4293 C LEU 557 77.169 14.246 8.5~4 1.00 29.06 ATOM 4294 O LEU 557 76.060 14.385 8.011 1.00 29.05 ATOM 4295 N TYR 558 77.717 13.065 8.807 1.00 29.43 ATOM 4297 CA TYR 558 77.018 11.823 8.573 1.00 28.02 ATOM 4298 CB TYR 558 77.813 10.918 7.632 1.00 27.83 ATOM 4299 CG TYR 558 77.969 11.414 6.203 1.00 31.70 ATOM 4300 CD1 TYR 558 78.966 10.893 5.383 1.00 32.90 ATOM 4301 CD1 TYR 558 79.121 11.315 4.073 1.00 32.69 ATOM 4302 CD2 TYR 558 77.122 12.386 5.666 1.00 30.23 ATOM 4303 CE2 TYR 558 77.271 12.815 4.350 1.00 29.97 ATOM 4304 CZ TYR 558 78.280 12.272 3.560 1.00 33.20 ATOM 4305 OH TYR 558 78.452 12.681 2.253 1.00 35.32 ATOM 4307 C TYR 558 76.848 11.131 9.932 1.00 28.42 ATOM 4308 O TYR 558 77.823 10.902 10.647 1.00 27.81 ATOM 4309 N VAL 559 75.601 10.870 10.313 1.00 29.20 ATOM 4311 CA VAL 559 75.286 10.175 11.564 1.00 29.17 ATOM 4312 CB VAL 559 74.102 10.832 12.329 1.00 28.53 ATOM 4313 CG1 VAL 559 73.802 10.036 13.607 1.00 27.08 ATOM 4314 CG2 VAL 559 74.456 12.281 12.687 1.00 23.27 ATOM 4315 C VAL 559 74.911 8.772 11.137 1.00 26.41 ATOM 4316 O VAL 559 73.834 8.536 10.593 1.00 25.91 ATOM 4317 N ILE 560 75.824 7.846 11.371 1.00 26.71 ATOM 4319 CA ILE 560 75.638 6.465 10.966 1.00 27.55 ATOM 4320 CB ILE 560 77.012 5.829 10.619 1.00 28.48 ATOM 4321 CG2 ILE 560 76.819 4.468 9.979 1.00 29.18 ATOM 4322 CG1 ILE 560 77.793 6.745 9.657 1.00 27.99 ATOM 4323 CD1 ILE 560 79.274 6.399 9.525 1.00 28.97 ATOM 4324 C ILE 560 74.917 5.644 12.034 1.00 29.17 ATOM 4325 O ILE 560 75.404 5.497 13.160 1.00 28.92 ATOM 4326 N VAL 561 73.743 5.129 11.681 1.00 28.60 ATOM 4328 CA VAL 561 72.957 4.325 12.606 1.00 28.58 ATOM 4329 CB VAL 561 71.634 5.061 13.047 1.00 27.53 ATOM 4330 CG1 VAL 561 71.951 6.400 13.701 1.00 22.44 ATOM 4331 CG2 VAL 561 70.697 5.246 11.874 1.00 23.19 ATOM 4332 C VAL 561 72.618 2.956 12.006 1.00 28.20 ATOM 4333 O VAL 561 72.875 2.694 10.825 1.00 27.99 ATOM 4334 N GLU 562 72.057 2.079 12.834 1.00 29.17 ATOM 4336 CA GLU 562 71.666 0.744 12.399 1.00 28.96 ATOM 4337 CB GLU 562 71.199 −0.086 13.589 1.00 27.34 ATOM 4338 CG GLU 562 72.308 −0.331 14.583 1.00 30.12 ATOM 4339 CD GLU 562 71.838 −1.075 15.808 1.00 32.29 ATOM 4340 OE1 GLU 562 72.526 −2.030 16.217 1.00 32.45 ATOM 4341 OE2 GLU 562 70.785 −0.702 16.362 1.00 30.16 ATOM 4342 C GLU 562 70.580 0.794 11.340 1.00 29.79 ATOM 4343 O GLU 562 69.690 1.653 11.386 1.00 29.75 ATOM 4344 N TYR 563 70.684 −0.106 10.369 1.00 30.51 ATOM 4346 CA TYR 563 69.735 −0.209 9.267 1.00 33.76 ATOM 4347 CB TYR 563 70.494 −0.602 7.988 1.00 31.04 ATOM 4348 CG TYR 563 69.624 −0.928 6.806 1.00 33.40 ATOM 4349 CD1 TYR 563 68.693 −0.019 6.340 1.00 33.07 ATOM 4350 CE1 TYR 563 67.908 −0.301 6.240 1.00 34.71 ATOM 4351 CD2 TYR 563 69.749 −2.141 6.147 1.00 34.61 ATOM 4352 CE2 TYR 563 68.970 −2.446 5.035 1.00 36.54 ATOM 4353 CZ TYR 563 68.047 −1.518 4.589 1.00 36.83 ATOM 4354 OH TYR 563 67.261 −1.805 3.501 1.00 38.81 ATOM 4356 C TYR 563 68.655 −1.269 9.588 1.00 36.14 ATOM 4357 O TYR 563 68.946 −2.365 10.023 1.00 37.70 ATOM 4358 N ALA 564 67.406 −0.948 9.309 1.00 37.87 ATOM 4360 CA ALA 564 66.276 −1.832 9.534 1.00 38.49 ATOM 4361 CB ALA 564 65.278 −1.167 10.458 1.00 42.57 ATOM 4362 C ALA 564 65.645 −2.153 8.179 1.00 39.65 ATOM 4363 O ALA 564 64.796 −1.423 7.687 1.00 39.74 ATOM 4364 N SER 565 66.039 −3.280 7.607 1.00 40.06 ATOM 4366 CA SER 565 65.567 −3.699 6.295 1.00 40.67 ATOM 4367 CB SER 565 66.267 −4.986 5.883 1.00 38.71 ATOM 4368 OG SER 565 66.107 −5.964 6.889 1.00 41.35 ATOM 4370 C SER 565 64.081 −3.884 6.106 1.00 42.17 ATOM 4371 O SER 565 63.585 −3.741 4.992 1.00 44.25 ATOM 4372 N LYS 566 63.360 −4.207 7.167 1.00 41.71 ATOM 4374 CA LYS 566 61.928 −4.427 7.015 1.00 40.22 ATOM 4375 CB LYS 566 61.525 −5.668 7.800 1.00 39.51 ATOM 4376 CG LYS 566 62.202 −6.910 7.226 1.00 41.48 ATOM 4377 CD LYS 566 62.113 −8.094 8.149 1.00 41.53 ATOM 4378 CE LYS 566 62.710 −9.312 7.491 1.00 41.18 ATOM 4379 NZ LYS 566 62.763 −10.458 8.438 1.00 46.17 ATOM 4383 C LYS 566 61.007 −3.220 7.263 1.00 40.47 ATOM 4384 O LYS 566 59.800 −3.367 7.486 1.00 42.68 ATOM 4385 N GLY 567 61.584 −2.026 7.167 1.00 38.90 ATOM 4387 CA GLY 567 60.826 −0.799 7.336 1.00 37.13 ATOM 4388 C GLY 567 60.199 −0.592 8.694 1.00 36.72 ATOM 4389 O GLY 567 60.644 −1.172 9.683 1.00 38.48 ATOM 4390 N ASN 568 59.191 0.273 8.753 1.00 35.77 ATOM 4392 CA ASN 568 58.518 0.549 10.015 1.00 35.36 ATOM 4393 CB ASN 568 57.883 1.957 10.045 1.00 36.30 ATOM 4394 CG ASN 568 56.635 2.088 9.169 1.00 38.06 ATOM 4395 OD1 ASN 568 55.623 1.421 9.383 1.00 38.66 ATOM 4396 ND2 ASN 568 56.686 3.010 8.221 1.00 37.29 ATOM 4399 C ASN 568 57.504 −0.532 10.341 1.00 33.04 ATOM 4400 O ASN 568 57.061 −1.265 9.461 1.00 32.10 ATOM 4401 N LEU 569 57.142 −0.612 11.617 1.00 33.59 ATOM 4403 CA LEU 569 56.199 −1.604 12.132 1.00 32.91 ATOM 4404 CB LEU 569 56.045 −1.428 13.647 1.00 33.84 ATOM 4405 CG LEU 569 55.088 −2.343 14.403 1.00 31.96 ATOM 4406 CD1 LEU 569 55.522 −3.797 14.216 1.00 33.20 ATOM 4407 CD2 LEU 569 55.089 −1.967 15.868 1.00 30.81 ATOM 4408 C LEU 569 54.820 −1.591 11.478 1.00 32.12 ATOM 4409 O LEU 569 54.214 −2.645 11.300 1.00 33.08 ATOM 4410 N ARG 570 54.315 −0.409 11.148 1.00 32.05 ATOM 4412 CA ARG 570 52.999 −0.293 10.529 1.00 35.21 ATOM 4413 CB ARG 570 52.659 1.173 10.256 1.00 36.77 ATOM 4414 CD ARG 570 51.282 1.370 9.653 1.00 43.11 ATOM 4425 C ARG 570 51.203 2.690 8.926 1.00 49.24 ATOM 4416 NE ARG 570 52.154 2.775 7.815 1.00 55.77 ATOM 4418 CZ ARG 570 52.995 3.790 7.619 1.00 58.89 ATOM 4419 NH1 ARG 570 53.016 4.820 8.463 1.00 61.61 ATOM 4422 NH2 ARG 570 53.804 3.786 6.566 1.00 59.16 ATOM 4425 C ARG 570 52.992 −1.063 9.220 1.00 35.16 ATOM 4426 O ARG 570 52.145 −1.922 8.990 1.00 35.50 ATOM 4427 N GLU 571 53.971 −0.760 8.383 1.00 36.29 ATOM 4429 CA GLU 571 54.111 −1.400 7.089 1.00 37.51 ATOM 4430 CB GLU 571 55.219 −0.701 6.308 1.00 41.27 ATOM 4431 CG GLU 571 54.945 0.778 6.110 1.00 49.88 ATOM 4432 CD GLU 571 56.087 1.516 5.436 1.00 57.58 ATOM 4433 OE1 GLU 571 57.264 1.122 5.636 1.00 60.59 ATOM 4434 OE2 GLU 571 55.804 2.504 4.714 1.00 61.14 ATOM 4435 C GLU 571 54.399 −2.896 7.228 1.00 36.24 ATOM 4436 O GLU 571 53.889 −3.716 6.459 1.00 34.22 ATOM 4437 N TYR 572 55.202 −3.238 8.232 1.00 35.98 ATOM 4439 CA TYR 572 55.570 −4.619 8.517 1.00 35.34 ATOM 4440 CB TYR 572 56.526 −4.656 9.714 1.00 30.94 ATOM 4441 CG TYR 572 56.959 −6.034 10.180 1.00 32.71 ATOM 4442 CD1 TYR 572 58.009 −6.714 9.547 1.00 32.33 ATOM 4443 CE1 TYR 572 58.464 −7.940 10.026 1.00 30.31 ATOM 4444 CD2 TYR 572 56.369 −6.626 11.303 1.00 33.43 ATOM 4445 CE2 TYR 572 56.813 −7.551 11.791 1.00 31.46 ATOM 4446 CZ TYP 572 57.864 −8.502 11.148 1.00 33.99 ATOM 4447 OH TYR 572 58.311 −9.706 11.640 1.00 36.30 ATOM 4449 C TYR 572 54.312 −5.425 8.826 1.00 37.26 ATOM 4450 O TYR 572 54.121 −6.530 8.314 1.00 36.91 ATOM 4451 N LEU 573 53.457 −4.850 9.665 1.00 36.82 ATOM 4453 CA LEU 573 52.208 −5.476 10.075 1.00 35.56 ATOM 4454 CB LEU 573 51.537 −4.629 11.165 1.00 34.03 ATOM 4455 CG LEU 573 52.238 −4.527 12.519 1.00 32.82 ATOM 4456 CD1 LEU 573 51.621 −3.423 13.377 1.00 28.95 ATOM 4457 CD2 LEU 573 52.168 −5.858 13.207 1.00 29.46 ATOM 4458 C LEU 573 51.237 −5.658 8.915 1.00 34.56 ATOM 4459 O LEU 573 50.670 −6.729 8.726 1.00 34.80 ATOM 4460 N GLN 574 51.030 −4.602 8.150 1.00 37.10 ATOM 4462 CA GLN 574 50.101 −4.666 7.031 1.00 41.15 ATOM 4463 CB GLN 574 49.875 −3.278 6.457 1.00 41.63 ATOM 4464 CG GLN 574 49.089 −2.375 7.366 1.00 43.13 ATOM 4465 CD GLN 574 49.063 −0.959 6.860 1.00 47.77 ATOM 4466 OE1 GLN 574 49.655 −0.647 5.827 1.00 50.00 ATOM 4467 NE2 GLN 574 48.378 −0.086 7.582 1.00 49.67 ATOM 4470 C GLN 574 50.529 −5.627 5.934 1.00 42.38 ATOM 4471 O GLN 574 49.685 −6.284 5.318 1.00 44.56 ATOM 4472 N ALA 575 51.835 −5.717 5.697 1.00 41.99 ATOM 4474 CA ALA 575 52.367 −6.608 4.676 1.00 41.29 ATOM 4475 CB ALA 575 53.841 −6.325 4.446 1.00 40.43 ATOM 4476 C ALA 575 52.186 −8.058 5.066 1.00 41.42 ATOM 4477 O ALA 575 52.392 −8.949 4.249 1.00 43.65 ATOM 4478 N ARG 576 51.815 −8.294 6.319 1.00 42.56 ATOM 4480 CA ARG 576 51.642 −9.646 6.824 1.00 42.51 ATOM 4481 CB ARG 576 52.676 −9.910 7.920 1.00 40.14 ATOM 4482 OG ARG 576 54.100 −9.896 7.377 1.00 40.32 ATOM 4483 CD ARG 576 55.172 −9.836 8.460 1.00 40.78 ATOM 4484 NE ARH 576 56.513 −9.783 7.874 1.00 42.13 ATOM 4486 CZ ARG 576 56.975 −8.785 7.120 1.00 40.73 ATOM 4487 NH1 ARG 576 56.215 −7.732 6.851 1.00 39.21 ATOM 4490 NH2 ARG 576 58.201 −8.846 6.622 1.00 37.62 ATOM 4493 C ARG 576 50.242 −9.931 7.326 1.00 44.48 ATOM 4494 O ARG 576 50.028 −10.869 8.098 1.00 46.84 ATOM 4495 N ARG 577 49.275 −9.146 6.866 1.00 46.26 ATOM 4497 CA ARG 577 47.893 −9.344 7.292 1.00 46.89 ATOM 4498 CB ARG 577 47.027 −8.170 6.845 1.00 46.16 ATOM 4499 CG ARG 577 47.189 −6.939 7.696 1.00 44.93 ATOM 4500 CD ARG 577 46.463 −5.766 7.080 1.00 44.60 ATOM 4501 NE ARG 577 46.284 −4.683 8.039 1.00 45.05 ATOM 4503 CZ ARG 577 45.612 −3.565 7.793 1.00 45.95 ATOM 4504 NH1 ARG 577 45.052 −3.372 6.606 1.00 47.39 ATOM 4507 NH2 ARG 577 45.466 −2.655 8.749 1.00 45.49 ATOM 4510 C ARG 577 47.334 −10.649 6.740 1.00 46.60 ATOM 4511 O ARG 577 47.478 −10.933 5.551 1.00 47.15 ATOM 4512 N GLN 594 53.312 −14.007 7.967 1.00 63.97 ATOM 4514 CA GLN 594 52.110 −14.068 8.799 1.00 63.06 ATOM 4515 CB GLN 594 51.175 −15.183 8.319 1.00 64.16 ATOM 4516 C GLN 594 52.501 −14.278 10.258 1.00 61.68 ATOM 4517 O GLN 594 53.101 −15.292 10.619 1.00 60.95 ATOM 4518 N LEU 595 52.140 −13.313 11.092 1.00 58.58 ATOM 4520 CA LEU 595 52.470 −13.335 12.505 1.00 55.58 ATOM 4521 CB LEU 595 52.619 −11.902 13.020 1.00 54.05 ATOM 4522 CG LEU 595 53.570 −11.074 12.153 1.00 56.23 ATOM 4523 CD1 LEU 595 53.496 −9.609 12.524 1.00 58.84 ATOM 4524 CD2 LEU 595 54.977 −11.596 12.301 1.00 55.93 ATOM 4525 C LEU 595 51.480 −14.093 13.372 1.00 53.77 ATOM 4526 O LEU 595 50.276 −14.046 13.139 1.00 54.31 ATOM 4527 N SER 596 52.012 −14.780 14.377 1.00 51.04 ATOM 4529 CA SER 596 51.206 −15.541 15.316 1.00 48.97 ATOM 4530 CB SER 596 52.004 −16.737 15.834 1.00 48.39 ATOM 4531 OG SER 596 52.945 −16.345 16.820 1.00 48.59 ATOM 4533 C SER 396 50.853 −14.641 16.488 1.00 47.56 ATOM 4534 O SER 596 51.470 −13.590 16.676 1.00 46.71 ATOM 4535 N SER 597 49.888 −15.070 17.292 1.00 47.11 ATOM 4537 CA SER 597 49.462 −14.315 18.461 1.00 47.88 ATOM 4538 CB SER 597 48.386 −15.084 19.229 1.00 50.66 ATOM 4539 OG SER 597 47.574 −15.839 18.343 1.00 57.08 ATOM 4541 C SER 597 50.666 −14.068 19.372 1.00 46.03 ATOM 4542 O SER 597 50.735 −13.045 20.047 1.00 46.49 ATOM 4543 N LYS 598 51.607 −15.007 19.399 1.00 46.08 ATOM 4545 CA LYS 598 52.798 −14.844 20.229 1.00 46.33 ATOM 4546 CB LYS 598 53.558 −16.163 20.384 1.00 46.67 ATOM 4547 CG LYS 598 54.449 −16.224 21.623 1.00 49.61 ATOM 4548 CD LYS 598 55.240 −17.539 21.668 1.00 53.69 ATOM 4549 CE LYS 598 55.899 −17.797 23.026 1.00 53.15 ATOM 4550 NZ LYS 598 54.891 −18.076 24.093 1.00 52.02 ATOM 4554 C LYS 598 53.706 −13.790 19.599 1.00 45.43 ATOM 4555 O LYS 598 54.292 −12.968 20.311 1.00 44.18 ATOM 4556 N ASP 599 53.780 −13.804 18.264 1.00 44.16 ATOM 4558 CA ASP 599 54.598 −12.851 17.513 1.00 43.46 ATOM 4559 CB ASP 599 54.523 −13.098 16.001 1.00 44.83 ATOM 4560 CG ASP 599 55.288 −14.336 15.560 1.00 48.24 ATOM 4561 OD1 ASP 599 56.228 −14.754 16.260 1.00 52.90 ATOM 4562 OD2 ASP 599 54.958 −14.894 14.493 1.00 51.43 ATOM 4563 C ASP 599 54.120 −11.437 17.796 1.00 42.71 ATOM 4564 O ASP 599 54.937 −10.550 18.059 1.00 45.00 ATOM 4565 N LEU 600 52.803 −11.235 17.776 1.00 37.69 ATOM 4567 CA LEU 600 52.246 −9.918 18.030 1.00 34.03 ATOM 4568 CB LEU 600 50.747 −9.882 17.747 1.00 34.06 ATOM 4569 CG LEU 600 50.332 −10.068 16.281 1.00 33.13 ATOM 4570 CD1 LEU 600 48.814 −9.992 16.190 1.00 37.38 ATOM 4571 CD2 LEU 600 50.974 −9.012 15.373 1.00 25.63 ATOM 4572 C LEU 600 52.537 −9.452 19.439 1.00 34.58 ATOM 4573 O LEU 600 52.910 −8.294 19.636 1.00 33.18 ATOM 4574 N VAL 601 52.415 −10.348 20.419 1.00 34.24 ATOM 4576 CA VAL 601 52.692 −9.969 21.808 1.00 35.80 ATOM 4577 CB VAL 601 52.214 −11.036 22.827 1.00 37.50 ATOM 4578 CG1 VAL 601 52.331 −10.483 24.252 1.00 38.08 ATOM 4579 CG2 VAL 601 50.766 −11.409 22.560 1.00 40.77 ATOM 4580 C VAL 601 54.198 −9.741 21.982 1.00 35.04 ATOM 4581 O VAL 601 54.634 −8.856 22.731 1.00 34.33 ATOM 4582 N SER 602 54.981 −10.531 21.262 1.00 32.58 ATOM 4584 CA SER 602 56.421 −10.421 21.307 1.00 36.01 ATOM 4585 CB SER 602 57.045 −11.504 20.439 1.00 38.43 ATOM 4586 OG SER 602 58.453 −11.387 20.419 1.00 43.36 ATOM 4588 C SER 602 56.809 −9.038 20.800 1.00 35.21 ATOM 4589 O SER 602 57.651 −8.363 21.394 1.00 35.03 ATOM 4590 N CYS 603 56.183 −8.614 19.707 1.00 34.15 ATOM 4592 CA CYS 603 56.438 −7.294 19.141 1.00 34.04 ATOM 4593 CB CYS 603 55.543 −7.055 17.925 1.00 33.45 ATOM 4594 SG CYS 603 55.653 −5.423 17.229 0.50 32.19 PRT1 ATOM 4595 C CYS 603 56.198 −6.211 20.191 1.00 32.79 ATOM 4596 O CYS 603 57.023 −5.316 20.362 1.00 33.36 ATOM 4597 N ALA 604 55.088 −6.321 20.917 3.00 31.31 ATOM 4599 CA ALA 604 54.743 −5.358 21.965 1.00 32.36 ATOM 4600 CB ALA 604 53.321 −5.610 22.481 2.00 32.01 ATOM 4601 C ALA 604 55.741 −5.394 23.128 1.00 32.83 ATOM 4602 O ALA 604 56.050 −4.358 23.727 1.00 30.89 ATOM 4603 N TYR 605 56.212 −6.592 23.465 1.00 32.95 ATOM 4605 CA TYR 605 57.189 −6.758 24.539 1.00 33.34 ATOM 4606 CB TYR 605 57.500 −8.236 24.737 1.00 32.58 ATOM 4607 CG TYR 605 58.640 −8.495 25.690 1.00 32.51 ATOM 4608 CD1 TYR 605 58.511 −8.236 27.053 1.00 33.50 ATOM 4609 CE1 TYR 605 59.556 −8.507 27.943 1.00 37.08 ATOM 4610 CD2 TYR 605 59.841 −9.026 25.230 1.00 34.22 ATOM 4611 CE2 TYR 605 60.896 −9.300 26.109 1.00 36.64 ATOM 4612 CZ TYR 605 60.746 −9.042 27.464 1.00 37.56 ATOM 4613 OH TYR 605 61.776 −9.342 28.336 1.00 38.08 ATOM 4615 C TYR 605 56.480 −6.006 24.191 1.00 32.42 ATOM 4616 O TYR 605 58.975 −5.203 24.991 1.00 33.34 ATOM 4617 N GLN 606 58.997 −6.261 22.989 1.00 30.61 ATOM 4619 CA GLN 606 60.218 −5.643 22.474 1.00 31.12 ATOM 4620 CB GLN 606 60.459 −6.143 21.058 1.00 30.57 ATOM 4621 CG GLN 606 61.044 −7.568 21.008 1.00 33.90 ATOM 4622 CD GLN 606 61.240 −8.080 19.593 1.00 32.17 ATOM 4623 OE1 GLN 606 62.155 −7.652 18.883 1.00 32.55 ATOM 4624 NE2 GLN 606 60.374 −8.998 29.171 1.00 33.10 ATOM 4627 C GLN 606 60.157 −4.114 22.487 1.00 31.69 ATOM 4628 O GLN 606 61.111 −3.453 22.910 1.00 31.18 ATOM 4629 N VAL 607 59.035 −3.564 22.020 1.00 29.50 ATOM 4631 CA VAL 607 58.816 −2.122 22.000 1.00 27.54 ATOM 4632 CB VAL 607 57.454 −1.751 21.306 1.00 26.79 ATOM 4633 OG1 VAL 607 57.131 −0.291 21.516 1.00 24.80 ATOM 4634 CG2 VAL 607 57.505 −2.050 19.815 1.00 22.95 ATOM 4635 C VAL 607 58.827 −1.576 23.432 1.00 28.30 ATOM 4636 O VAL 607 59.469 −0.548 23.705 1.00 28.32 ATOM 4637 N ALA 608 58.110 −2.247 24.340 1.00 27.21 ATOM 4639 CA ALA 608 58.061 −1.805 25.735 1.00 26.54 ATOM 4640 CB ALA 608 57.070 −2.649 26.550 1.00 26.70 ATOM 4641 C ALA 608 59.457 −1.85C 26.368 1.00 25.97 ATOM 4642 O ALA 608 59.802 −0.993 27.183 1.00 25.88 ATOM 4643 N ARG 609 60.250 −2.848 25.994 1.00 26.02 ATOM 4645 CA ARG 609 61.606 −2.977 26.512 1.00 30.44 ATOM 4646 CB ARG 609 62.234 −4.285 26.058 1.00 34.09 ATOM 4647 CG ARG 609 61.642 −5.516 26.682 1.00 39.24 ATOM 4648 CD ARG 609 62.659 −6.615 26.615 1.00 42.75 ATOM 4649 NE ARG 609 63.405 −6.704 27.860 1.00 45.52 ATOM 4651 CZ ARG 609 64.525 −7.405 28.019 1.00 46.24 ATOM 4652 NH1 ARG 609 65.055 −8.079 27.001 1.00 41.48 ATOM 4655 NH2 ARG 609 65.079 −7.482 29.225 1.00 47.49 ATOM 4658 C ARG 609 62.478 −1.829 26.015 1.00 34.20 ATOM 4659 O ARG 609 63.265 −1.255 26.788 1.00 35.24 ATOM 4660 N GLY 610 62.368 −1.528 24.717 1.00 33.25 ATOM 4662 CA GLY 610 63.130 −0.439 24.138 1.00 29.57 ATOM 4663 C GLY 610 62.802 0.814 24.908 1.00 29.31 ATOM 4664 O GLY 610 63.695 1.543 25.335 1.00 27.46 ATOM 4665 N MET 611 61.507 1.020 25.147 1.00 31.07 ATOM 4667 CA MET 611 61.016 2.178 25.889 1.00 30.09 ATOM 4668 CB MET 611 59.493 2.280 25.782 1.00 29.51 ATOM 4669 CG MET 611 58.997 2.655 24.404 1.00 28.21 ATOM 4670 SD MET 611 59.760 4.175 23.787 1.00 29.00 ATOM 4671 CE MET 611 59.350 5.335 25.039 1.00 25.91 ATOM 4672 C MET 611 61.439 2.189 27.361 1.00 30.47 ATOM 4673 O MET 611 61.734 3.242 27.919 1.00 29.43 ATOM 4674 N GLU 612 61.429 1.031 28.002 1.00 31.97 ATOM 4676 CA GLU 612 61.836 0.947 29.402 1.00 35.34 ATOM 4677 CB GLU 612 61.707 −0.490 29.904 1.00 36.17 ATOM 4678 CG GLU 612 62.305 −0.729 31.278 1.00 34.87 ATOM 4679 CD GLU 612 62.259 −2.185 31.705 1.00 32.68 ATOM 4680 OE1 GLU 612 62.641 −3.070 30.904 1.00 35.01 ATOM 4681 OE2 GLU 612 61.848 −2.443 32.858 1.00 36.56 ATOM 4682 C GLU 612 63.296 1.425 29.490 1.00 35.26 ATOM 4683 O GLU 612 63.677 2.162 30.417 1.00 31.21 ATOM 4684 N TYR 613 64.092 1.040 28.491 1.00 36.10 ATOM 4686 CA TYR 613 65.491 1.458 28.440 1.00 34.76 ATOM 4687 CB TYR 613 66.249 0.788 27.301 1.00 31.15 ATOM 4688 CG TYR 613 67.700 1.195 27.284 1.00 34.28 ATOM 4689 CD1 TYR 613 68.600 0.654 28.207 1.00 36.50 ATOM 4690 CE1 TYR 613 69.949 1.035 28.219 1.00 38.20 ATOM 4691 CD2 TYR 613 68.179 2.135 26.366 1.00 32.99 ATOM 4692 CE2 TYR 613 69.520 2.526 26.372 1.00 33.32 ATOM 4693 CZ TYR 613 70.399 1.968 27.302 1.00 36.59 ATOM 4694 OH TYR 613 71.721 2.340 27.333 1.00 35.73 ATOM 4696 C TYR 613 65.583 2.970 28.273 1.00 34.03 ATOM 4697 O TYR 613 66.231 3.643 29.075 1.00 35.26 ATOM 4698 N LEU 614 64.916 3.503 27.250 1.00 31.78 ATOM 4700 CA LEU 614 64.945 4.937 26.998 1.00 29.50 ATOM 4701 CB LEU 614 64.095 5.297 25.775 1.00 28.26 ATOM 4702 CG LEU 614 64.564 4.742 24.422 1.00 31.29 ATOM 4703 CD1 LEU 614 63.564 5.089 23.321 1.00 28.09 ATOM 4704 CD2 LEU 614 65.951 5.282 24.079 1.00 29.52 ATOM 4705 C LEU 614 64.489 5.715 28.224 1.00 32.49 ATOM 4706 O LEU 614 65.108 6.717 28.598 1.00 31.73 ATOM 4707 N ALA 615 63.431 5.232 28.872 1.00 33.06 ATOM 4709 CA ALA 615 62.906 5.870 30.070 1.00 35.16 ATOM 4710 CB ALA 615 61.598 5.192 30.511 1.00 36.64 ATOM 4711 C ALA 615 63.942 5.838 31.202 1.00 35.36 ATOM 4712 O ALA 615 64.065 6.805 31.952 1.00 36.80 ATOM 4713 N SER 616 64.690 4.739 31.315 1.00 35.91 ATOM 4715 CA SER 616 65.716 4.621 32.354 1.00 35.78 ATOM 4716 CB SER 616 66.287 3.199 32.424 1.00 32.52 ATOM 4717 OG SER 616 67.133 2.899 31.324 1.00 29.64 ATOM 4719 C SER 616 66.832 5.623 32.063 1.00 37.48 ATOM 4720 O SER 616 67.556 6.048 32.967 1.00 38.76 ATOM 4721 N LYS 617 66.971 5.980 30.790 1.00 34.74 ATOM 4723 CA LYS 617 67.973 6.931 30.357 1.00 32.44 ATOM 4724 CB LYS 617 68.540 6.520 28.998 1.00 32.94 ATOM 4725 CG LYS 617 69.330 5.232 29.041 1.00 32.64 ATOM 4726 CD LYS 617 70.539 5.402 29.933 1.00 38.45 ATOM 4727 CE LYS 617 71.252 4.091 30.139 1.00 40.84 ATOM 4728 NZ LYS 617 72.552 4.306 30.812 1.00 46.49 ATOM 4732 C LYS 617 67.376 8.325 30.281 1.00 33.29 ATOM 4733 O LYS 617 67.909 9.188 29.598 1.00 33.95 ATOM 4734 N LYS 618 66.245 8.528 30.952 1.00 34.87 ATOM 4736 CA LYS 618 65.569 9.822 30.997 1.00 35.44 ATOM 4737 CB LYS 618 66.512 10.868 31.581 1.00 40.44 ATOM 4738 CG LYS 618 67.192 10.446 32.877 1.00 48.19 ATOM 4739 CD LYS 618 66.234 10.363 34.037 1.00 55.47 ATOM 4740 CE LYS 618 66.962 9.939 35.310 1.00 61.56 ATOM 4741 NZ LYS 618 66.070 10.032 36.514 1.00 68.82 ATOM 4745 C LYS 618 65.015 10.327 29.663 1.00 35.62 ATOM 4746 O LYS 618 64.557 11.463 29.569 1.00 36.44 ATOM 4747 N CYS 619 65.006 9.472 28.647 1.00 34.24 ATOM 4749 CA CYS 619 64.525 9.848 27.323 1.00 31.62 ATOM 4750 CB CYS 619 65.279 9.033 26.263 1.00 31.17 ATOM 4751 SG CYS 619 64.816 9.306 24.541 1.00 30.02 ATOM 4752 C CYS 619 63.004 9.701 27.149 1.00 30.45 ATOM 4753 O CYS 619 62.418 8.649 27.388 1.00 29.24 ATOM 4754 N ILE 620 62.359 10.798 26.800 1.00 30.14 ATOM 4756 CA ILE 620 60.935 10.822 26.542 1.00 31.76 ATOM 4757 CB ILE 620 60.268 12.040 27.193 1.00 31.26 ATOM 4758 CG2 ILE 620 58.799 12.116 26.774 1.00 31.66 ATOM 4759 CG1 ILE 620 60.392 11.957 28.712 1.00 29.71 ATOM 4760 CD1 ILE 620 60.016 13.236 29.396 1.00 27.40 ATOM 4761 C ILE 620 60.864 10.961 25.023 1.00 31.86 ATOM 4762 O ILE 620 61.384 11.920 24.465 1.00 32.70 ATOM 4763 N HIS 621 60.249 9.986 24.366 1.00 31.70 ATOM 4765 CA HIS 621 60.133 9.973 22.906 1.00 32.12 ATOM 4766 CB HIS 621 59.708 8.578 22.430 1.00 29.61 ATOM 4767 CG HIS 621 59.903 8.344 20.961 1.00 28.62 ATOM 4768 CD2 HIS 621 60.511 7.336 20.300 1.00 27.49 ATOM 4769 ND1 HIS 621 59.373 9.168 19.988 1.00 30.08 ATOM 4771 CE1 HIS 621 59.637 8.669 18.795 1.00 25.00 ATOM 4772 NE2 HIS 621 60.325 7.554 18.956 1.00 26.55 ATOM 4774 C HIS 621 59.194 11.026 22.321 1.00 34.51 ATOM 4775 O HIS 621 59.466 11.570 21.251 1.00 36.79 ATOM 4776 N ARG 622 58.048 11.248 22.960 1.00 35.26 ATOM 4778 CA ARG 622 57.068 12.239 22.490 1.00 34.68 ATOM 4779 CB ARG 622 57.705 13.628 22.370 1.00 33.43 ATOM 4780 CG ARG 622 58.285 14.135 23.674 1.00 31.52 ATOM 4781 CD ARG 622 58.781 15.563 23.570 0.50 27.82 ATOM 4782 NE ARG 622 59.216 16.050 24.876 0.50 28.82 ATOM 4784 CZ ARG 622 60.362 15.715 25.463 0.50 30.41 ATOM 4785 NH1 ARG 622 61.215 14.891 24.860 0.50 31.15 ATOM 4788 NH2 ARG 622 60.640 16.168 26.680 0.50 30.83 ATOM 4791 C ARG 622 56.283 11.891 21.213 1.00 34.71 ATOM 4792 O ARG 622 55.289 12.544 20.912 1.00 35.58 ATOM 4793 N ASP 623 56.719 10.884 20.459 1.00 34.90 ATOM 4795 CA ASP 623 55.986 10.468 19.261 1.00 34.30 ATOM 4796 CB ASP 623 56.443 11.212 17.994 1.00 36.76 ATOM 4797 CG ASP 623 55.535 10.918 16.772 1.00 43.35 ATOM 4798 OD1 ASP 623 55.980 11.131 15.624 1.00 47.64 ATOM 4799 OD2 ASP 623 54.376 10.469 16.954 1.00 43.30 ATOM 4800 C ASP 623 56.094 8.967 19.051 1.00 32.24 ATOM 4801 O ASP 623 56.406 8.494 17.957 1.00 31.19 ATOM 4802 N LEU 624 55.895 8.209 20.118 1.00 32.27 ATOM 4804 CA LEU 624 55.964 6.759 20.005 1.00 33.18 ATOM 4805 CB LEU 624 56.013 6.118 21.390 1.00 31.16 ATOM 4806 CG LEU 624 56.019 4.592 21.452 1.00 32.74 ATOM 4807 CD1 LEU 624 57.257 4.020 20.765 1.00 30.64 ATOM 4808 CD2 LEU 624 55.974 4.177 22.904 1.00 34.51 ATOM 4809 C LEU 624 54.738 6.274 19.217 1.00 35.18 ATOM 4810 O LEU 624 53.589 6.511 19.612 1.00 35.72 ATOM 4811 N ALA 625 54.997 5.632 18.084 1.00 32.37 ATOM 4813 CA ALA 625 53.946 5.113 17.223 1.00 30.60 ATOM 4814 CB ALA 625 53.447 6.205 16.298 1.00 25.26 ATOM 4815 C ALA 625 54.618 4.020 16.427 1.00 29.87 ATOM 4816 O ALA 625 55.839 3.978 16.378 1.00 32.01 ATOM 4817 N ALA 626 53.834 3.163 15.779 1.00 30.12 ATOM 4819 CA ALA 626 54.373 2.057 14.978 1.00 29.62 ATOM 4820 CB ALA 626 53.231 1.159 14.441 1.00 27.11 ATOM 4821 C ALA 626 55.255 2.552 13.838 1.00 26.57 ATOM 4822 O ALA 626 56.193 1.871 13.434 1.00 26.29 ATOM 4823 N ARG 627 54.935 3.730 13.317 1.00 26.74 ATOM 4825 CA ARG 627 55.706 4.352 12.244 1.00 28.73 ATOM 4826 CB ARG 627 55.056 5.671 11.827 1.00 29.62 ATOM 4827 CG ARG 627 54.894 6.659 12.972 1.00 31.84 ATOM 4828 CD ARG 627 54.435 8.032 12.485 1.00 38.54 ATOM 4829 NE ARG 627 53.987 8.878 13.590 1.00 38.59 ATOM 4831 CZ ARG 627 52.745 8.879 14.064 1.00 39.55 ATOM 4832 NH1 ARG 627 51.822 8.094 13.525 1.00 35.96 ATOM 4835 NH2 ARG 627 52.447 9.604 15.127 1.00 41.05 ATOM 4838 C ARG 627 57.151 4.632 12.676 1.00 30.79 ATOM 4839 O ARG 627 58.058 4.687 11.838 1.00 30.16 ATOM 4840 N ASN 628 57.347 4.822 13.985 1.00 30.31 ATOM 4842 CA ASN 628 58.661 5.109 14.550 1.00 28.50 ATOM 4843 CB ASN 628 58.587 6.257 15.549 1.00 27.84 ATOM 4844 CG ASN 628 58.369 7.571 14.868 1.00 31.41 ATOM 4845 OD1 ASN 628 58.893 7.796 13.782 1.00 33.45 ATOM 4846 ND2 ASN 628 57.551 8.429 15.460 1.00 28.53 ATOM 4849 C ASN 628 59.352 3.919 15.169 1.00 28.10 ATOM 4850 O ASN 628 60.232 4.076 16.021 1.00 28.64 ATOM 4851 N VAL 629 58.887 2.733 14.803 1.00 27.79 ATOM 4853 CA VAL 629 59.484 1.482 15.253 1.00 28.30 ATOM 4854 CB VAL 629 58.475 0.577 15.983 1.00 25.38 ATOM 4855 CG1 VAL 629 59.118 −0.753 16.284 1.00 23.07 ATOM 4856 CG2 VAL 629 57.980 1.246 17.265 1.00 22.48 ATOM 4857 C VAL 629 59.925 0.810 13.949 1.00 28.69 ATOM 4858 O VAL 629 59.114 0.616 13.043 1.00 27.07 ATOM 4859 N LEU 630 61.220 0.542 13.823 1.00 29.54 ATOM 4861 CA LEU 630 61.749 −0.081 12.616 1.00 30.17 ATOM 4862 CB LEU 630 62.999 0.659 12.142 1.00 29.62 ATOM 4863 CG LEU 630 62.831 2.180 12.035 1.00 29.14 ATOM 4864 CD1 LEU 630 64.121 2.795 11.579 1.00 29.83 ATOM 4865 CD2 LEU 630 61.693 2.543 11.086 1.00 32.59 ATOM 4866 C LEU 630 62.036 −1.541 12.899 1.00 30.50 ATOM 4867 O LEU 630 62.290 −1.910 14.042 1.00 31.06 ATOM 4868 N VAL 631 61.966 −2.376 11.866 1.00 33.03 ATOM 4870 CA VAL 631 62.174 −3.813 12.022 1.00 31.83 ATOM 4871 CB VAL 631 60.902 −4.605 11.582 1.00 29.48 ATOM 4872 CG1 VAL 631 61.017 −6.067 11.980 1.00 29.39 ATOM 4873 CG2 VAL 631 59.644 −3.984 12.196 1.00 25.38 ATOM 4874 C VAL 631 63.379 −4.242 11.196 1.00 32.37 ATOM 4875 O VAL 631 63.508 −3.865 10.024 1.00 33.57 ATOM 4876 N THR 632 64.285 −4.987 11.820 1.00 34.39 ATOM 4878 CA THR 632 65.504 −5.453 11.145 1.00 35.84 ATOM 4879 CB THR 632 66.659 −5.685 12.148 1.00 33.11 ATOM 4880 OG1 THR 632 66.328 −6.774 13.020 1.00 34.88 ATOM 4882 CG2 THR 632 66.922 −4.426 12.972 1.00 28.85 ATOM 4883 C THR 632 65.272 −6.738 10.350 1.00 37.63 ATOM 4884 O THR 632 64.195 −7.347 10.439 1.00 37.20 ATOM 4885 N GLU 633 66.289 −7.163 9.600 1.00 39.78 ATOM 4887 CA GLU 633 66.182 −8.379 8.794 1.00 43.30 ATOM 4888 CB GLU 633 67.437 −8.590 7.933 1.00 46.66 ATOM 4889 CG GLU 633 67.336 −9.729 6.876 1.00 51.37 ATOM 4890 CD GLU 633 66.490 −9.404 5.622 1.00 54.30 ATOM 4891 OE1 GLU 633 65.859 −8.327 5.523 1.00 55.85 ATOM 4892 OE2 GLU 633 66.460 −10.256 4.710 1.00 55.95 ATOM 4893 C GLU 633 65.919 −9.592 9.677 1.00 42.72 ATOM 4894 O GLU 633 65.360 −10.582 9.222 1.00 45.10 ATOM 4895 N ASP 634 66.287 −9.494 10.949 1.00 42.83 ATOM 4897 CA ASP 634 66.075 −10.585 11.884 1.00 43.03 ATOM 4898 CB ASP 634 67.324 −10.809 12.743 1.00 49.02 ATOM 4899 CG ASP 634 68.539 −11.240 11.916 1.00 55.95 ATOM 4900 OD1 ASP 634 68.462 −12.292 11.237 1.00 59.10 ATOM 4901 OD2 ASP 634 69.568 −10.525 11.943 1.00 59.41 ATOM 4902 C ASP 634 64.848 −10.340 12.751 1.00 41.75 ATOM 4903 O ASP 634 64.737 −10.873 13.847 1.00 42.79 ATOM 4904 N ASN 635 63.937 −9.508 12.257 1.00 42.51 ATOM 4906 CA ASN 635 62.686 −9.186 12.939 1.00 42.53 ATOM 4907 CB ASN 635 61.768 −10.417 12.992 1.00 45.07 ATOM 4908 CG ASN 635 61.483 −10.985 11.624 1.00 46.54 ATOM 4909 OD1 ASN 635 60.868 −10.336 10.786 1.00 49.77 ATOM 4910 ND2 ASN 635 61.949 −12.192 11.383 1.00 49.29 ATOM 4913 C ASN 635 62.801 −8.577 14.331 1.00 40.51 ATOM 4914 O ASN 635 61.939 −8.800 15.187 1.00 41.80 ATOM 4915 N VAL 636 63.844 −7.795 14.561 1.00 37.98 ATOM 4917 CA VAL 636 64.016 −7.164 15.856 1.00 33.92 ATOM 4918 CB VAL 636 65.517 −7.005 16.195 1.00 32.21 ATOM 4919 CG1 VAL 636 65.697 −6.284 17.530 1.00 31.40 ATOM 4920 CG2 VAL 636 66.169 −8.367 16.242 1.00 30.93 ATOM 4921 C VAL 636 63.349 −5.797 15.811 1.00 31.85 ATOM 4922 O VAL 636 63.531 −5.061 14.849 1.00 33.47 ATOM 4923 N MET 637 62.525 −5.492 16.807 1.00 31.69 ATOM 4925 CA MET 637 61.860 −4.194 16.879 1.00 31.44 ATOM 4926 CB MET 637 60.642 −4.241 17.820 1.00 34.97 ATOM 4927 CG MET 637 59.559 −5.264 17.455 1.00 36.80 ATOM 4928 SD MET 637 58.860 −5.048 15.803 1.00 35.45 ATOM 4929 CE MET 637 59.030 −6.709 15.116 1.00 32.12 ATOM 4930 C MET 637 62.874 −3.209 17.454 1.00 31.86 ATOM 4931 O MET 637 63.512 −3.496 18.479 1.00 29.47 ATOM 4932 N LYS 638 62.985 −2.041 16.820 1.00 30.87 ATOM 4934 CA LYS 638 63.915 −0.994 17.244 1.00 29.66 ATOM 4935 CB LYS 638 65.161 −0.983 16.349 1.00 27.51 ATOM 4936 CG LYS 638 66.171 −2.059 16.691 1.00 27.29 ATOM 4937 CD LYS 638 67.370 −1.984 15.781 1.00 28.55 ATOM 4938 CE LYS 638 68.409 −3.029 16.150 1.00 24.75 ATOM 4939 NZ LYS 638 68.964 −2.785 17.498 1.00 25.59 ATOM 4943 C LYS 638 63.283 0.383 17.215 1.00 27.72 ATOM 4944 O LYS 638 62.918 0.869 16.146 1.00 27.66 ATOM 4945 N ILE 639 63.163 1.004 18.387 1.00 26.21 ATOM 4947 CA ILE 639 62.597 2.343 18.501 1.00 26.27 ATOM 4948 CB ILE 639 62.580 2.862 19.965 1.00 26.52 ATOM 4949 CG2 ILE 639 61.896 4.206 20.017 1.00 21.50 ATOM 4950 CG1 ILE 639 61.918 1.854 20.926 1.00 25.70 ATOM 4951 CD1 ILE 639 60.496 1.494 20.599 1.00 25.62 ATOM 4952 C ILE 639 63.505 3.288 17.718 1.00 29.56 ATOM 4953 O ILE 639 64.730 3.281 17.906 1.00 27.74 ATOM 4954 N ALA 640 62.897 4.101 16.857 1.00 27.91 ATOM 4956 CA ALA 640 63.620 5.071 16.042 1.00 28.79 ATOM 4957 CB ALA 640 63.377 4.796 14.563 1.00 26.74 ATOM 4958 C ALA 640 63.164 6.487 16.385 1.00 28.91 ATOM 4959 O ALA 640 62.087 6.683 16.956 1.00 28.67 ATOM 4960 N ASP 641 64.007 7.464 16.067 1.00 28.25 ATOM 4962 CA ASP 641 63.708 8.876 16.296 1.00 30.80 ATOM 4963 CB ASP 641 62.520 9.319 15.428 1.00 33.44 ATOM 4964 CG ASP 641 62.869 9.393 13.948 1.00 38.01 ATOM 4965 OD1 ASP 641 64.002 9.001 13.574 1.00 42.41 ATOM 4966 OD2 ASP 641 62.006 9.847 13.160 1.00 41.74 ATOM 4967 C ASP 641 63.501 9.311 17.745 1.00 29.07 ATOM 4968 O ASP 641 62.847 10.309 18.020 1.00 28.42 ATOM 4969 N PHE 642 64.138 8.604 18.663 1.00 29.69 ATOM 4971 CA PHE 642 64.036 8.914 20.074 1.00 29.62 ATOM 4972 CB PHE 642 64.347 7.656 20.890 1.00 27.18 ATOM 4973 CG PHE 642 65.702 7.058 20.603 1.00 23.96 ATOM 4974 CD1 PHE 642 66.848 7.559 21.219 1.00 23.66 ATOM 4975 CD2 PHE 642 65.828 5.974 19.742 1.00 24.08 ATOM 4976 CE1 PHE 642 68.090 6.992 20.980 1.00 23.02 ATOM 4977 CE2 PHE 642 67.069 5.403 19.501 1.00 23.20 ATOM 4978 CZ PHE 642 68.200 5.909 20.121 1.00 21.68 ATOM 4979 C PHE 642 64.948 10.075 20.502 1.00 32.99 ATOM 4980 O PHE 642 64.755 10.664 21.574 1.00 32.10 ATOM 4981 N GLY 643 65.940 10.396 19.671 1.00 34.66 ATOM 4983 CA GLY 643 66.869 11.463 20.003 1.00 35.29 ATOM 4984 C GLY 643 66.639 12.755 19.250 1.00 39.13 ATOM 4985 O GLY 643 67.464 13.666 19.333 1.00 39.83 ATOM 4986 N LEU 644 65.520 12.850 18.532 1.00 42.26 ATOM 4988 CA LEU 644 65.202 14.043 17.745 1.00 46.25 ATOM 4989 CB LEU 644 63.935 13.843 16.911 1.00 44.59 ATOM 4990 CG LEU 644 63.911 12.839 15.763 1.00 43.00 ATOM 4991 CD1 LEU 644 62.653 13.068 14.940 1.00 42.61 ATOM 4992 CD2 LEU 644 65.119 13.016 14.889 1.00 45.65 ATOM 4993 C LEU 644 65.037 15.298 18.578 1.00 49.59 ATOM 4994 O LEU 644 64.391 15.281 19.623 1.00 51.90 ATOM 4995 N ALA 645 65.585 16.401 18.080 1.00 52.08 ATOM 4997 CA ALA 645 65.495 17.677 18.777 1.00 54.71 ATOM 4998 CB ALA 645 66.414 18.699 18.124 1.00 54.38 ATOM 4999 C ALA 645 64.053 18.184 18.790 1.00 55.44 ATOM 5000 O ALA 645 63.534 18.582 19.832 1.00 56.69 ATOM 5001 N ASP 652 52.389 21.543 14.759 1.00 73.74 ATOM 5003 CA ASP 652 51.207 21.745 13.934 1.00 73.83 ATOM 5004 CB ASP 652 51.601 21.995 12.472 1.00 73.22 ATOM 5005 CG ASP 652 50.398 22.241 11.569 1.00 72.95 ATOM 5006 OD1 ASP 652 49.354 22.715 12.065 1.00 73.71 ATOM 5007 OD2 ASP 652 50.497 21.956 10.357 1.00 73.02 ATOM 5008 C ASP 652 50.321 20.514 14.042 1.00 75.11 ATOM 5009 O ASP 652 50.568 19.495 13.394 1.00 75.96 ATOM 5010 N TYR 653 49.272 20.628 14.849 1.00 75.57 ATOM 5012 CA TYR 653 48.348 19.524 15.064 1.00 75.68 ATOM 5013 CB TYR 653 47.274 19.914 16.088 1.00 76.85 ATOM 5014 CG TYR 653 47.771 19.995 17.519 1.00 79.55 ATOM 5015 CD1 TYR 653 46.983 20.567 18.518 1.00 80.89 ATOM 5016 CE1 TYR 653 47.438 20.648 19.836 1.00 83.02 ATOM 5017 CD2 TYR 653 49.032 19.503 17.874 1.00 80.87 ATOM 5018 CE2 TYR 653 49.496 19.578 19.183 1.00 81.70 ATOM 5019 CZ TYR 653 48.698 20.152 20.160 1.00 83.09 ATOM 5020 OH TYR 653 49.165 20.243 21.451 1.00 83.73 ATOM 5022 C TYR 653 47.685 19.038 13.787 1.00 75.03 ATOM 5023 O TYR 653 47.232 17.897 13.711 1.00 75.97 ATOM 5024 N TYR 654 47.679 19.885 12.767 1.00 73.85 ATOM 5026 CA TYR 654 47.039 19.538 11.507 1.00 73.32 ATOM 5027 CB TYR 654 46.276 20.750 10.972 1.00 71.97 ATOM 5028 CG TYR 654 45.259 21.276 11.954 1.00 70.94 ATOM 5029 CD1 TYR 654 45.659 21.801 13.185 1.00 71.41 ATOM 5030 CE1 TYR 654 44.733 22.234 14.121 1.00 73.60 ATOM 5031 CD2 TYR 654 43.899 21.206 11.680 1.00 71.81 ATOM 5032 CE2 TYR 654 42.956 21.642 12.610 1.00 74.81 ATOM 5033 CZ TYR 654 43.380 22.152 13.832 1.00 74.84 ATOM 5034 OH TYR 654 42.457 22.571 14.769 1.00 76.60 ATOM 5036 C TYR 654 47.975 18.967 10.446 1.00 73.82 ATOM 5037 O TYR 654 47.545 18.671 9.329 1.00 74.25 ATOM 5038 N LYS 655 49.249 18.806 10.784 1.00 74.04 ATOM 5040 CA LYS 655 50.195 18.256 9.827 1.00 75.41 ATOM 5041 CB LYS 655 51.626 18.680 10.164 1.00 78.45 ATOM 5042 CG LYS 655 52.647 18.198 9.151 1.00 83.01 ATOM 5043 CD LYS 655 54.062 18.589 9.537 1.00 87.72 ATOM 5044 CE LYS 655 55.076 17.813 8.703 1.00 91.45 ATOM 5045 NZ LYS 655 56.489 18.133 9.074 1.00 94.17 ATOM 5049 C LYS 655 50.075 16.736 9.832 1.00 75.50 ATOM 5050 O LYS 655 50.245 16.092 10.872 1.00 75.90 ATOM 5051 N LYS 656 49.750 16.173 8.672 1.00 75.26 ATOM 5053 CA LYS 656 49.597 14.730 8.533 1.00 74.97 ATOM 5054 CB LYS 656 48.723 14.406 7.323 1.00 75.40 ATOM 5055 CG LYS 656 47.266 14.753 7.519 1.00 76.87 ATOM 5056 CD LYS 656 46.489 14.535 6.239 1.00 80.75 ATOM 5057 CE LYS 656 45.001 14.655 6.483 1.00 83.60 ATOM 5058 NZ LYS 656 44.236 14.637 5.204 1.00 87.14 ATOM 5062 C LYS 656 50.939 14.016 8.414 1.00 74.58 ATOM 5063 0 LYS 656 51.904 14.578 7.897 1.00 75.01 ATOM 5064 N GLY 660 49.137 9.764 5.736 1.00 59.18 ATOM 5066 CA GLY 660 48.106 10.781 5.848 1.00 56.19 ATOM 5067 C GLY 660 47.407 10.761 7.192 1.00 55.31 ATOM 5068 O GLY 660 46.289 11.263 7.328 1.00 56.96 ATOM 5069 N ARG 661 48.059 10.163 8.183 1.00 53.02 ATOM 5071 CA ARG 661 47.493 10.083 9.527 1.00 49.80 ATOM 5072 CB ARG 661 47.944 8.799 10.229 1.00 51.79 ATOM 5073 CG ARG 661 47.683 7.523 9.450 1.00 50.59 ATOM 5074 CD ARG 661 47.822 6.323 10.367 1.00 53.68 ATOM 5075 NE ARG 661 47.714 5.044 9.665 1.00 52.66 ATOM 5077 CZ ARG 661 47.928 3.863 10.236 1.00 51.73 ATOM 5078 NH1 ARG 661 48.264 3.794 11.518 1.00 50.23 ATOM 5081 NH2 ARG 661 47.800 2.751 9.528 1.00 52.58 ATOM 5084 C ARG 661 47.915 11.297 10.346 1.00 44.80 ATOM 5085 O ARG 661 48.865 11.998 9.986 1.00 43.61 ATOM 5086 N LEU 662 47.221 11.528 11.453 1.00 40.74 ATOM 5088 CA LEU 662 47.518 12.654 12.333 1.00 37.88 ATOM 5089 CB LEU 662 46.234 13.415 12.671 1.00 36.19 ATOM 5090 CG LEU 662 45.515 14.074 11.499 1.00 35.32 ATOM 5091 CD1 LEU 662 44.045 14.278 11.831 1.00 31.05 ATOM 5092 CD2 LEU 662 46.217 15.383 11.156 1.00 34.37 ATOM 5093 C LEU 662 48.162 12.170 13.622 1.00 35.34 ATOM 5094 O LEU 662 47.529 11.479 14.417 1.00 33.06 ATOM 5095 N PRO 663 49.441 12.518 13.843 1.00 36.39 ATOM 5096 CD PRO 663 50.375 13.113 12.868 1.00 37.57 ATOM 5097 CA PRO 663 50.158 12.107 15.054 1.00 36.39 ATOM 5098 CB PRO 663 51.516 12.787 14.885 1.00 36.98 ATOM 5099 CG PRO 663 51.728 12.657 13.401 1.00 38.48 ATOM 5100 C PRO 663 49.477 12.491 16.371 1.00 35.47 ATOM 5101 O PRO 663 49.699 11.841 17.392 1.00 35.08 ATOM 5102 N VAL 664 48.646 13.532 16.362 1.00 34.28 ATOM 5104 CA VAL 664 47.951 13.931 17.583 1.00 34.43 ATOM 5105 CB VAL 664 47.038 15.181 17.376 1.00 36.92 ATOM 5106 CG1 VAL 664 47.885 16.408 17.160 1.00 37.55 ATOM 5107 CG2 VAL 664 46.091 14.989 16.186 1.00 38.28 ATOM 5108 C VAL 664 47.137 12.749 18.120 1.00 33.03 ATOM 5109 O VAL 664 46.908 12.641 19.318 1.00 34.62 ATOM 5110 N LYS 665 46.803 11.809 17.236 1.00 32.47 ATOM 5112 CA LYS 665 46.040 10.631 17.614 1.00 30.71 ATOM 5113 CB LYS 665 45.456 9.958 16.370 1.00 29.59 ATOM 5114 CG LYS 665 44.324 10.774 15.768 1.00 29.64 ATOM 5115 CD LYS 665 43.927 10.334 14.367 1.00 31.86 ATOM 5116 CE LYS 665 42.664 11.056 13.899 1.00 30.42 ATOM 5117 NZ LYS 665 42.296 10.720 12.486 1.00 26.50 ATOM 5121 C LYS 665 46.801 9.644 18.498 1.00 32.23 ATOM 5122 O LYS 665 46.230 8.659 18.955 1.00 30.04 ATOM 5123 N TRP 666 48.080 9.915 18.748 1.00 31.38 ATOM 5125 CA TRP 666 48.886 9.068 19.619 1.00 32.32 ATOM 5126 CB TPP 666 50.204 8.682 18.945 1.00 31.07 ATOM 5127 CG TRP 666 50.078 7.530 18.006 1.00 28.26 ATOM 5128 CD2 TPP 666 49.531 7.559 16.684 1.00 27.07 ATOM 5129 CR2 TRP 666 49.630 6.257 16.163 1.00 26.71 ATOM 5130 CR3 TRP 666 48.982 8.569 15.882 1.00 26.56 ATOM 5131 OD1 TRP 666 50.473 6.238 18.234 1.00 24.97 ATOM 5132 NE1 TRP 666 50.206 5.469 17.132 1.00 27.38 ATOM 5134 CZ2 TEP 666 49.190 5.929 14.874 1.00 27.22 ATOM 5135 CZ3 TRP 666 48.548 8.248 14.599 1.00 30.14 ATOM 5136 CH2 TRP 666 48.658 6.934 14.107 1.00 26.64 ATOM 5137 C TRP 666 49.203 9.802 20.913 1.00 33.84 ATOM 5138 O TRP 666 49.688 9.202 21.873 1.00 32.82 ATOM 5139 N MET 667 48.905 11.099 20.929 1.00 35.75 ATOM 5141 CA MET 667 49.180 11.960 22.069 1.00 37.60 ATOM 5142 CB MET 667 49.150 13.423 21.641 1.00 41.95 ATOM 5143 CG MET 667 50.487 13.975 21.226 1.00 48.44 ATOM 5144 SD MET 667 50.384 15.728 20.919 1.00 55.33 ATOM 5145 CE MET 667 50.711 15.745 19.183 1.00 49.29 ATOM 5146 C MET 667 48.294 11.802 23.289 1.00 38.98 ATOM 5147 O MET 667 47.066 11.699 23.183 1.00 39.18 ATOM 5148 N ALA 668 48.933 11.824 24.456 1.00 38.72 ATOM 5150 CA ALA 668 48.231 11.728 25.727 1.00 37.82 ATOM 5151 CB ALA 668 49.224 11.527 26.857 1.00 38.49 ATOM 5152 C ALA 668 47.497 13.051 25.891 1.00 38.16 ATOM 5153 O ALA 668 47.937 14.072 25.363 1.00 37.21 ATOM 5154 N PRO 669 46.383 13.062 26.644 1.00 39.78 ATOM 5155 CD PRO 669 45.785 11.931 27.367 1.00 40.08 ATOM 5156 CA PRO 669 45.598 14.281 26.858 1.00 40.68 ATOM 5157 CB PRO 669 44.474 13.806 27.782 1.00 42.15 ATOM 5158 CG PRO 669 44.346 12.352 27.446 1.00 42.56 ATOM 5159 C PRO 669 46.398 15.432 27.484 1.00 42.69 ATOM 5160 O PRO 669 46.320 16.566 27.019 1.00 42.14 ATOM 5161 N GLU 670 47.168 15.153 28.532 1.00 43.21 ATOM 5163 CA GLU 670 47.956 16.211 29.160 1.00 44.62 ATOM 5164 CB GLU 670 48.651 15.719 30.429 1.00 44.95 ATOM 5165 CG GLU 670 49.824 14.782 30.197 1.00 45.54 ATOM 5166 CD GLU 670 49.422 13.332 30.079 1.00 42.72 ATOM 5167 OE1 GLU 670 50.332 12.481 30.066 1.00 41.43 ATOM 5168 OE2 GLU 670 48.212 13.036 30.015 1.00 44.44 ATOM 5169 C GLU 670 48.993 16.772 28.195 1.00 44.88 ATOM 5170 O GLU 670 49.248 17.968 28.194 1.00 45.08 ATOM 5171 N ALA 671 49.565 15.908 27.358 1.00 44.75 ATOM 5173 CA ALA 671 50.573 16.323 26.392 1.00 45.92 ATOM 5174 CB ALA 671 51.256 15.095 25.766 1.00 44.10 ATOM 5175 C ALA 671 49.944 17.193 25.314 1.00 47.96 ATOM 5176 O ALA 671 50.526 18.192 24.894 1.00 49.16 ATOM 5177 N LEU 672 48.729 16.836 24.917 1.00 49.84 ATOM 5179 CA LEU 672 47.989 17.554 23.881 1.00 50.74 ATOM 5180 CB LEU 672 46.926 16.619 23.289 1.00 53.20 ATOM 5181 CG LEU 672 46.184 16.989 22.004 1.00 55.26 ATOM 5182 CD1 LEU 672 47.153 17.155 20.856 1.00 57.12 ATOM 5183 CD2 LEU 672 45.203 15.895 21.680 1.00 52.86 ATOM 5184 C LEU 672 47.327 18.826 24.408 1.00 50.79 ATOM 5185 O LEU 672 47.302 19.855 23.736 1.00 50.95 ATOM 5186 N PHE 673 46.792 18.751 25.618 1.00 52.07 ATOM 5188 CA PHE 673 46.111 19.884 26.226 1.00 54.39 ATOM 5189 CB PHE 673 44.892 19.396 27.019 1.00 51.21 ATOM 5190 CG PEE 673 43.871 18.656 26.186 1.00 48.49 ATOM 5191 CD1 PEE 673 43.304 17.473 26.646 1.00 47.79 ATOM 5192 CD2 PHE 673 43.470 19.149 24.949 1.00 49.04 ATOM 5193 CR1 PHE 673 42.349 16.789 25.888 1.00 47.90 ATOM 5194 CR2 PHE 673 42.511 18.473 24.182 1.00 49.71 ATOM 5195 CZ PHE 673 41.952 17.288 24.655 1.00 46.86 ATOM 5196 C PHE 673 47.007 20.741 27.123 1.00 58.25 ATOM 5197 O PHE 673 47.000 21.971 27.034 1.00 60.52 ATOM 5198 N ASP 674 47.784 20.094 27.983 1.00 59.63 ATOM 5200 CA ASP 674 48.652 20.815 28.905 1.00 62.11 ATOM 5201 CB ASP 674 48.568 20.196 30.307 1.00 63.81 ATOM 5202 CG ASP 674 47.143 20.015 30.791 1.00 66.46 ATOM 5203 OD1 ASP 674 46.815 18.901 31.247 1.00 66.70 ATOM 5204 OD2 ASP 674 46.354 20.981 30.722 1.00 68.77 ATOM 5205 C ASP 674 50.119 20.852 28.482 1.00 63.36 ATOM 5206 O ASP 674 50.979 21.175 29.310 1.00 64.11 ATOM 5207 N ARG 675 50.410 20.486 27.228 1.00 62.94 ATOM 5209 CA ARG 675 51.789 20.456 26.706 1.00 60.75 ATOM 5210 CB ARG 675 52.277 21.874 26.360 1.00 60.56 ATOM 5211 CG ARG 675 51.474 22.560 25.261 1.00 63.67 ATOM 5212 CD ARG 675 51.986 23.970 24.964 1.00 66.99 ATOM 5213 NE ARG 675 53.308 23.980 24.337 1.00 69.34 ATOM 5215 CZ ARG 675 54.063 25.068 24.173 1.00 68.48 ATOM 5216 NE1 ARG 675 53.637 26.254 24.590 1.00 65.81 ATOM 5219 NH2 ARG 675 55.254 24.965 23.593 1.00 68.76 ATOM 5222 C ARG 675 52.750 19.793 27.700 1.00 58.06 ATOM 5223 O ARG 675 53.933 20.130 27.766 1.00 59.30 ATOM 5224 N ILE 676 52.221 18.859 28.483 1.00 55.62 ATOM 5226 CA ILE 676 52.992 18.141 29.489 1.00 54.09 ATOM 5227 CB ILE 676 52.154 17.921 30.765 1.00 52.69 ATOM 5228 CG2 ILE 676 52.749 16.811 31.629 1.00 49.38 ATOM 5229 CG1 ILE 676 52.049 19.230 31.540 1.00 53.15 ATOM 5230 CD1 ILE 676 51.306 19.103 32.845 1.00 57.79 ATOM 5231 C ILE 676 53.468 16.796 28.953 1.00 53.83 ATOM 5232 O ILE 676 52.668 15.891 28.730 1.00 54.87 ATOM 5233 N TYR 677 54.773 16.671 28.745 1.00 51.76 ATOM 5235 CA TYR 677 55.343 15.436 28.236 1.00 49.42 ATOM 5236 CB TYR 677 56.232 15.722 27.031 1.00 51.33 ATOM 5237 CG TYR 677 55.466 16.181 25.809 1.00 56.22 ATOM 5238 CD1 TYR 677 55.158 17.529 25.619 1.00 56.12 ATOM 5239 CE1 TYR 677 54.491 17.960 24.479 1.00 56.18 ATOM 5240 CD2 TYR 677 55.078 15.269 24.823 1.00 58.13 ATOM 5241 CE2 TYR 677 54.411 15.689 23.679 1.00 57.65 ATOM 5242 CZ TYR 677 54.125 17.035 23.512 1.00 58.23 ATOM 5243 OH TYR 677 53.504 17.457 22.360 1.00 61.71 ATOM 5245 C TYR 677 56.136 14.730 29.316 1.00 46.46 ATOM 5246 O THR 677 56.983 15.335 29.970 1.00 48.65 ATOM 5247 N THR 678 55.818 13.464 29.537 1.00 41.73 ATOM 5249 CA THR 678 56.498 12.664 30.535 1.00 39.83 ATOM 5250 C3 THR 678 55.680 12.593 31.861 1.00 41.78 ATOM 5251 OG1 THR 678 54.462 11.867 31.642 1.00 45.77 ATOM 5253 CG2 THR 678 55.342 13.988 32.383 1.00 41.84 ATOM 5254 C THR 678 56.661 11.242 30.011 1.00 37.46 ATOM 5255 O THR 678 56.258 10.917 28.897 1.00 37.51 ATOM 5256 N HIS 679 57.264 10.388 30.825 1.00 36.36 ATOM 5258 CA HIS 679 57.423 9.003 30.457 1.00 35.91 ATOM 5259 CB HIS 679 58.348 8.294 31.439 1.00 35.05 ATOM 5260 CG HIS 679 59.761 8.798 31.404 1.00 37.68 ATOM 5261 CD2 HIS 679 60.453 9.569 32.278 1.00 37.89 ATOM 5262 ND1 HIS 679 60.632 8.507 30.380 1.00 37.49 ATOM 5264 CE1 HIS 679 61.803 9.071 30.621 1.00 39.58 ATOM 5265 NE2 HIS 679 61.721 9.722 31.766 1.00 39.81 ATOM 5267 C HIS 679 56.032 8.376 30.441 1.00 36.76 ATOM 5268 O HIS 679 55.771 7.458 29.660 1.00 37.16 ATOM 5269 N GLN 680 55.126 8.908 31.264 1.00 36.27 ATOM 5271 CA GLN 680 53.754 8.407 31.332 1.00 37.71 ATOM 5272 CB GLN 680 53.069 8.815 32.640 1.00 40.95 ATOM 5273 CG GLN 680 53.645 8.128 33.884 1.00 45.23 ATOM 5274 CD GLN 680 53.676 6.595 33.780 1.00 44.44 ATOM 5275 OE1 GLN 680 52.669 5.925 33.996 1.00 42.76 ATOM 5276 NE2 GLN 680 54.846 6.043 33.464 1.00 40.57 ATOM 5279 C GLN 680 52.927 8.842 30.121 1.00 37.54 ATOM 5280 O GLN 680 51.950 8.185 29.765 1.00 37.93 ATOM 5281 N SER 681 53.282 9.961 29.504 1.00 36.38 ATOM 5283 CA SER 681 52.563 10.367 28.306 1.00 38.05 ATOM 5284 CB SER 681 52.857 11.819 27.940 1.00 41.41 ATOM 5285 OG SER 681 54.239 12.069 27.938 1.00 42.92 ATOM 5287 C SER 681 52.991 9.421 27.178 1.00 37.92 ATOM 5288 0 SER 681 52.205 9.148 26.2S3 1.00 37.21 ATOM 5289 N ASP 682 54.237 8.932 27.248 1.00 34.77 ATOM 5291 CA ASP 682 54.750 7.972 26.267 1.00 31.99 ATOM 5292 CB ASP 682 56.243 7.683 26.481 1.00 31.08 ATOM 5293 CG ASP 682 57.165 8.638 25.721 1.00 33.63 ATOM 5294 OD1 ASP 682 58.386 8.503 25.920 1.00 32.35 ATOM 5295 OD2 ASP 682 56.707 9.500 24.930 1.00 29.46 ATOM 5296 C ASP 682 53.969 6.672 26.457 1.00 31.54 ATOM 5297 O ASP 682 53.675 5.971 25.493 1.00 29.94 ATOM 5298 N VAL 683 53.677 6.334 27.712 1.00 30.48 ATOM 5300 CA VAL 683 52.913 5.126 28.023 1.00 32.94 ATOM 5301 CB VAL 683 52.731 4.939 29.572 1.00 33.94 ATOM 5302 CG1 VAL 683 51.635 3.905 29.872 1.00 32.71 ATOM 5303 CG2 VAL 683 54.042 4.474 30.209 1.00 27.41 ATOM 5304 C VAL 683 51.545 5.164 27.299 1.00 32.27 ATOM 5305 O VAL 683 51.106 4.158 26.733 1.00 30.54 ATOM 5306 N TRP 684 50.902 6.332 27.282 1.00 32.57 ATOM 5308 CA TRP 684 49.616 6.477 26.600 1.00 32.76 ATOM 5309 CB TRP 684 49.060 7.895 26.765 1.00 33.67 ATOM 5310 CG TRP 684 47.855 8.210 25.891 1.00 38.22 ATOM 5311 CD2 TRP 684 46.503 8.435 26.328 1.00 39.96 ATOM 5312 CE2 TRP 684 45.734 8.735 25.177 1.00 39.59 ATOM 5313 CE3 TRP 684 45.869 8.416 27.578 1.00 39.26 ATOM 5314 CD1 TRP 684 47.842 8.373 24.528 1.00 39.02 ATOM 5315 NE1 TRP 684 46.576 8.687 24.096 1.00 38.42 ATOM 5317 CZ2 TRP 684 44.362 9.011 25.240 1.00 36.62 ATOM 5318 CZ3 TRP 684 44.502 8.691 27.641 1.00 40.70 ATOM 5319 CH2 TRP 684 43.766 8.982 26.475 1.00 40.57 ATOM 5320 C TRP 684 49.819 6.158 25.125 1.00 31.98 ATOM 5321 O TRP 684 49.066 5.367 24.557 1.00 32.43 ATOM 5322 N SER 685 50.859 6.748 24.529 1.00 29.63 ATOM 5324 CA SER 685 51.195 6.531 23.119 1.00 28.62 ATOM 5325 CB SER 685 52.457 7.296 22.751 1.00 24.72 ATOM 5326 OG SER 685 52.323 8.664 23.072 1.00 30.04 ATOM 5328 C SER 685 51.414 5.055 22.825 1.00 27.91 ATOM 5329 O SER 685 51.022 4.555 21.767 1.00 28.60 ATOM 5330 N PHE 686 52.063 4.372 23.763 1.00 27.96 ATOM 5332 CA PHE 686 52.333 2.947 23.662 1.00 27.03 ATOM 5333 CB PHE 686 53.163 2.499 24.868 1.00 25.79 ATOM 5334 CG PHE 686 53.440 1.029 24.890 1.00 26.25 ATOM 5335 CD1 PHE 686 54.252 0.451 23.923 1.00 27.32 ATOM 5336 CD2 PHE 686 52.839 0.208 25.841 1.00 26.22 ATOM 5337 CE1 PHE 686 54.464 −0.930 23.900 1.00 25.87 ATOM 5338 CE2 PHE 686 53.046 −1.170 25.828 1.00 24.37 ATOM 5339 CZ PHE 686 53.856 −1.740 24.854 1.00 26.42 ATOM 5340 C PHE 686 51.003 2.160 23.596 1.00 28.82 ATOM 5341 O PHE 686 50.912 1.129 22.914 1.00 26.74 ATOM 5342 N GLY 687 49.991 2.636 24.324 1.00 29.52 ATOM 5344 CA GLY 687 48.688 1.982 24.302 1.00 31.57 ATOM 5345 C GLY 687 48.095 2.036 22.896 1.00 30.73 ATOM 5346 O GLY 687 47.490 1.069 22.414 1.00 29.83 ATOM 5347 N VAL 688 48.269 3.179 22.238 1.00 29.06 ATOM 5349 CA VAL 688 47.777 3.350 20.879 1.00 28.93 ATOM 5350 CB VAL 688 47.800 4.831 20.424 1.00 27.24 ATOM 5351 CG1 VAL 688 47.211 4.963 19.020 1.00 28.29 ATOM 5352 CG2 VAL 688 46.990 5.691 21.404 1.00 26.96 ATOM 5353 C VAL 688 48.612 2.475 19.951 1.00 28.49 ATOM 5354 O VAL 688 48.080 1.866 19.024 1.00 28.84 ATOM 5355 N LEU 689 49.905 2.350 20.252 1.00 27.99 ATOM 5357 CA LEU 689 50.804 1.512 19.461 1.00 26.14 ATOM 5358 CB LEU 689 52.268 1.688 19.911 1.00 27.31 ATOM 5359 CG LEU 689 53.368 1.014 19.065 1.00 26.60 ATOM 5360 CD1 LEU 689 54.688 1.767 19.175 1.00 28.19 ATOM 5361 CD2 LEU 689 53.567 −0.401 19.475 1.00 25.55 ATOM 5362 C LEU 689 50.362 0.053 19.605 1.00 26.48 ATOM 5363 O LEU 689 50.377 −0.686 18.626 1.00 27.06 ATOM 5364 N LEU 690 49.953 −0.344 20.816 1.00 28.55 ATOM 5366 CA LEU 690 49.465 −1.708 21.085 1.00 29.16 ATOM 5367 CB LEU 690 49.070 −1.888 22.560 1.00 31.40 ATOM 5368 CG LEU 690 50.114 −2.085 23.667 1.00 31.49 ATOM 5369 CD1 LEU 690 49.427 −2.028 25.026 1.00 34.09 ATOM 5370 CD2 LEU 690 50.821 −3.410 23.491 1.00 30.84 ATOM 5371 C LEU 690 48.240 −1.958 20.220 1.00 26.51 ATOM 5372 O LEU 690 48.088 −3.023 19.631 1.00 25.15 ATOM 5373 N TPP 691 47.376 −0.954 20.139 1.00 28.51 ATOM 5375 CA TRP 691 46.169 −1.049 19.319 1.00 29.56 ATOM 5376 CB TRP 691 45.332 0.227 19.465 1.00 28.91 ATOM 5377 CG TRP 691 43.992 0.169 18.759 1.00 30.95 ATOM 5378 CD2 TRP 691 43.718 0.556 17.406 1.00 29.87 ATOM 5379 CE2 TRP 691 42.337 0.367 17.189 1.00 31.97 ATOM 5380 CE3 TRP 691 44.505 1.049 16.358 1.00 27.72 ATOM 5381 CD1 TRP 691 42.796 −0.231 19.292 1.00 30.68 ATOM 5382 NE1 TRP 691 41.797 −0.111 18.355 1.00 33.68 ATOM 5384 CZ2 TRP 691 41.729 0.652 15.967 1.00 29.42 ATOM 5385 CZ3 TRP 691 43.906 1.327 15.154 1.00 27.13 ATOM 5386 CH2 TRP 691 42.523 1.129 14.965 1.00 29.18 ATOM 5387 C TRP 691 46.564 −1.289 17.856 1.00 28.78 ATOM 5388 O TRP 691 45.996 −2.156 17.194 1.00 27.64 ATOM 5389 N GLU 692 47.564 −0.543 17.380 1.00 29.83 ATOM 5391 CA GLU 692 48.078 −0.669 16.018 1.00 28.08 ATOM 5392 CB GLU 692 49.267 0.262 15.790 1.00 26.40 ATOM 5393 CG GLU 692 48.945 1.735 15.680 1.00 26.45 ATOM 5394 CD GLU 692 50.183 2.561 15.369 1.00 29.47 ATOM 5395 OE1 GLU 692 50.938 2.886 16.320 1.00 29.66 ATOM 5396 OE2 GLU 692 50.413 2.875 14.182 1.00 29.44 ATOM 5397 C GLU 692 48.563 −2.082 15.761 1.00 30.07 ATOM 5398 O GLU 692 48.385 −2.612 14.665 1.00 30.18 ATOM 5399 N ILE 693 49.244 −2.663 16.746 1.00 29.87 ATOM 5401 CA ILE 693 49.754 −4.024 16.608 1.00 29.51 ATOM 5402 CB ILE 693 50.632 −4.443 17.828 1.00 28.18 ATOM 5403 CG2 ILE 693 51.037 −5.907 17.706 1.00 27.45 ATOM 5404 CG1 ILE 693 51.907 −3.594 17.890 1.00 26.99 ATOM 5405 CD1 ILE 693 52.663 −3.747 19.194 1.00 25.37 ATOM 5406 C ILE 693 48.603 −5.023 16.452 1.00 29.21 ATOM 5407 O ILE 693 48.568 −5.807 15.512 1.00 27.89 ATOM 5408 N PHE 694 47.623 −4.942 17.336 1.00 31.33 ATOM 5410 CA PHE 694 46.523 −5.888 17.279 1.00 34.41 ATOM 5411 CB PHE 694 45.958 −6.114 18.687 1.00 35.37 ATOM 5412 CG PHE 694 46.978 −6.717 19.621 1.00 35.60 ATOM 5413 CD1 PHE 694 47.606 −5.942 20.586 1.00 37.23 ATOM 5414 CD2 PHE 694 47.424 −8.024 19.426 1.00 35.59 ATOM 5415 CE1 PHE 694 48.669 −6.460 21.333 1.00 36.39 ATOM 5416 CE2 PHE 694 48.484 −8.546 20.170 1.00 35.34 ATOM 5417 CZ PHE 694 49.110 −7.762 21.118 1.00 35.71 ATOM 5418 C PHE 694 45.481 −5.715 16.176 1.00 34.41 ATOM 5419 O PHE 694 44.623 −6.579 15.982 1.00 34.48 ATOM 5420 N THR 695 45.617 −4.637 15.404 1.00 33.03 ATOM 5422 CA THR 695 44.742 −4.375 14.263 1.00 31.81 ATOM 5423 CB THR 695 44.113 −2.957 14.278 1.00 29.75 ATOM 5424 OG1 THR 695 45.142 −1.961 14.218 1.00 30.72 ATOM 5426 CG2 THR 695 43.254 −2.759 15.524 1.00 29.40 ATOM 5427 C THR 695 45.596 −4.533 13.011 1.00 31.44 ATOM 5428 O THR 695 45.153 −4.241 11.906 1.00 33.00 ATOM 5429 N LEU 696 46.832 −4.987 13.209 1.00 31.24 ATOM 5431 CA LEU 696 47.799 −5.199 12.134 1.00 31.36 ATOM 5432 CB LEU 696 47.421 −6.418 11.291 1.00 33.53 ATOM 5433 CG LEU 696 47.270 −7.741 12.042 1.00 33.00 ATOM 5434 CD1 LEU 696 47.010 −8.838 11.052 1.00 35.50 ATOM 5435 CD2 LEU 696 48.515 −8.061 12.830 1.00 36.09 ATOM 5436 C LEU 696 48.066 −3.976 11.249 1.00 30.84 ATOM 5437 O LEU 696 48.135 −4.067 10.024 1.00 28.23 ATOM 5438 N GLY 697 48.302 −2.839 11.890 1.00 31.54 ATOM 5440 CA GLY 697 48.591 −1.632 11.141 1.00 33.87 ATOM 5441 C GLY 697 47.375 −0.765 10.924 1.00 32.77 ATOM 5442 O GLY 697 47.322 −9.042 9.994 1.00 33.90 ATOM 5443 N GLY 698 46.392 −0.921 11.797 1.00 33.29 ATOM 5445 CA GLY 698 45.187 −0.122 11.681 1.00 32.66 ATOM 5446 C GLY 698 45.408 1.368 11.877 1.00 30.57 ATOM 5447 O GLY 698 46.336 1.803 12.553 1.00 27.36 ATOM 5448 N SER 699 44.517 2.148 11.285 1.00 30.92 ATOM 5450 CA SER 699 44.552 3.595 11.376 1.00 32.19 ATOM 5451 CB SER 699 44.062 4.202 10.058 1.00 34.24 ATOM 5452 OG SER 699 44.019 5.616 10.123 1.00 38.67 ATOM 5454 C SER 699 43.644 4.014 12.538 1.00 31.81 ATOM 5455 O SER 699 42.431 3.759 12.525 1.00 31.39 ATOM 5456 N PRO 700 44.228 4.597 13.594 1.00 31.82 ATOM 5457 CD PRO 700 45.645 4.842 13.919 1.00 28.82 ATOM 5458 CA PRO 700 43.353 4.992 14.697 1.00 31.31 ATOM 5459 CB PRO 700 44.345 5.341 15.809 1.00 31.31 ATOM 5460 CG PRO 700 45.552 5.800 15.061 1.00 30.41 ATOM 5461 C PRO 700 42.484 6.170 14.295 1.00 31.19 ATOM 5462 O PRO 700 42.899 7.021 13.510 1.00 29.93 ATOM 5463 N TYR 701 41.235 6.144 14.736 1.00 32.69 ATOM 5465 CA TYR 701 40.291 7.223 14.445 1.00 32.54 ATOM 5466 CB TYR 701 40.650 8.416 15.323 1.00 34.47 ATOM 5467 CG TYR 701 40.512 8.141 16.794 1.00 39.16 ATOM 5468 CD1 TYR 701 41.542 8.433 17.683 1.00 44.31 ATOM 5469 CE1 TYR 701 41.372 8.241 19.060 1.00 46.65 ATOM 5470 CD2 TYR 701 39.321 7.642 17.307 1.00 41.21 ATOM 5471 CE2 TYR 701 39.147 7.447 18.657 1.00 45.05 ATOM 5472 CZ TYR 701 40.164 7.750 19.535 1.00 47.24 ATOM 5473 OH TYR 701 39.949 7.590 20.886 1.00 52.18 ATOM 5475 C TYR 701 40.215 7.655 12.972 1.00 30.56 ATOM 5476 O TYR 701 40.379 8.836 12.647 1.00 29.73 ATOM 5477 N PRO 702 39.928 6.712 10.068 1.00 30.38 ATOM 5478 CD PRO 702 39.659 5.278 12.261 1.00 30.22 ATOM 5479 CA PRO 702 39.847 7.071 10.642 1.00 28.87 ATOM 5480 CB PRO 702 39.693 5.722 9.948 1.00 29.63 ATOM 5481 CG PRO 702 39.007 4.889 10.959 1.00 30.99 ATOM 5482 C PRO 702 38.722 8.048 10.283 1.00 30.88 ATOM 5483 O PRO 702 37.557 7.843 10.636 1.00 33.98 ATOM 5484 N GLY 703 39.100 9.116 9.584 1.00 29.03 ATOM 5486 CA GLY 703 38.154 10.134 9.169 1.00 28.98 ATOM 5487 C GLY 703 37.893 11.169 10.244 1.00 29.69 ATOM 5488 O GLY 703 37.074 12.068 10.048 1.00 31.71 ATOM 5489 N VAL 704 38.579 11.040 11.378 1.00 30.74 ATOM 5491 CA VAL 704 38.416 11.951 12.509 1.00 32.06 ATOM 5492 CB VAL 704 38.582 11.208 13.860 1.00 31.70 ATOM 5493 CG1 VAL 704 38.522 12.197 15.044 1.00 30.29 ATOM 5494 CG2 VAL 704 37.506 10.144 14.005 1.00 31.56 ATOM 5495 C VAL 704 39.430 13.087 12.449 1.00 33.72 ATOM 5496 O VAL 704 40.634 12.867 12.548 1.00 35.31 ATOM 5497 N PRO 705 38.957 14.309 12.200 1.00 34.23 ATOM 5498 CD PRO 705 37.594 14.692 11.787 1.00 33.20 ATOM 5499 CA PRO 705 39.875 15.443 12.135 1.00 33.73 ATOM 5500 CB PRO 705 39.053 16.495 11.394 1.00 34.93 ATOM 5501 CG PRO 705 37.647 16.187 11.831 1.00 36.93 ATOM 5502 C PRO 705 40.280 15.879 13.543 1.00 33.25 ATOM 5503 O PRO 705 39.651 15.490 14.532 1.00 31.71 ATOM 5504 N VAL 706 41.322 16.697 13.623 1.00 34.46 ATOM 5506 CA VAL 706 41.852 17.176 14.900 1.00 36.99 ATOM 5507 CB VAL 706 42.923 18.261 14.687 1.00 39.01 ATOM 5508 CG1 VAL 706 43.577 18.618 16.017 1.00 40.33 ATOM 5509 CG2 VAL 706 43.961 17.786 13.673 1.00 38.61 ATOM 5510 C VAL 706 40.826 17.716 15.895 1.00 35.65 ATOM 5511 O VAL 706 40.823 17.319 17.065 1.00 33.55 ATOM 5512 N GLU 707 39.955 18.605 15.426 1.00 36.74 ATOM 5514 CA GLU 707 38.941 19.220 16.278 1.00 37.20 ATOM 5515 CB GLU 707 38.129 20.242 15.482 1.00 38.98 ATOM 5516 C GLU 707 38.014 18.188 16.900 1.00 38.46 ATOM 5517 O GLU 707 37.634 18.295 18.074 1.00 39.04 ATOM 5518 N GLU 708 37.681 17.170 16.115 1.00 37.81 ATOM 5520 CA GLU 708 36.802 16.105 16.571 1.00 37.70 ATOM 5521 CB GLU 708 36.316 15.289 15.378 1.00 40.73 ATOM 5522 CG GLU 708 35.459 16.091 14.413 1.00 43.44 ATOM 5523 CD GLU 708 34.235 16.677 15.084 1.00 51.52 ATOM 5524 OE1 GLU 708 33.629 16.007 15.961 1.00 50.14 ATOM 5525 OE2 GLU 708 33.882 17.824 14.732 1.00 59.46 ATOM 5526 C GLU 708 37.506 15.223 17.588 1.00 36.53 ATOM 5527 O GLU 708 36.897 14.782 18.567 1.00 36.80 ATOM 5528 N LEU 709 38.799 14.993 17.376 1.00 35.69 ATOM 5530 CA LEU 709 39.584 14.179 18.301 1.00 35.48 ATOM 5531 CB LEU 709 41.039 14.044 17.830 1.00 34.84 ATOM 5532 CG LEU 709 41.921 13.250 18.802 1.00 32.41 ATOM 5533 CD1 LEU 709 41.608 11.787 18.674 1.00 30.10 ATOM 5534 CD2 LEU 709 43.378 13.514 18.560 1.00 29.93 ATOM 5535 C LEU 709 39.568 14.842 19.673 1.00 35.58 ATOM 5536 O LEU 709 39.377 14.177 20.694 1.00 35.43 ATOM 5537 N PHE 710 39.792 16.150 19.686 1.00 36.79 ATOM 5539 CA PHE 710 39.800 16.918 20.927 1.00 40.58 ATOM 5540 CB PHE 710 39.944 18.413 20.637 1.00 42.55 ATOM 5541 CG PHE 710 41.308 18.808 20.162 1.00 46.38 ATOM 5542 CD1 PHE 710 42.392 17.942 20.313 1.00 47.29 ATOM 5543 CD2 PHE 710 41.515 20.050 19.580 1.00 47.93 ATOM 5544 CE1 PHE 710 43.659 18.312 19.892 1.00 51.21 ATOM 5545 CE2 PHE 710 42.781 20.435 19.155 1.00 50.89 ATOM 5546 CZ PHE 710 43.859 19.562 19.312 1.00 53.31 ATOM 5547 C PHE 710 38.517 16.676 21.694 1.00 40.14 ATOM 5548 O PHE 710 38.543 16.446 22.898 1.00 39.86 ATOM 5549 N LYS 711 37.399 16.705 20.977 1.00 41.02 ATOM 5551 CA LYS 711 36.101 16.479 21.584 1.00 38.66 ATOM 5552 CB LYS 711 34.985 16.803 20.580 1.00 40.75 ATOM 5553 CG LYS 711 33.601 16.727 21.181 1.00 46.99 ATOM 5554 CD LYS 711 32.522 17.174 20.218 1.00 50.71 ATOM 5555 CE LYS 711 31.163 16.733 20.739 1.00 52.53 ATOM 5556 NZ LYS 711 30.041 17.194 19.884 1.00 57.76 ATOM 5560 C LYS 711 35.990 15.046 22.120 1.00 38.06 ATOM 5561 O LYS 711 35.535 14.831 23.250 1.00 36.29 ATOM 5562 N LEU 712 36.431 14.066 21.330 1.00 38.10 ATOM 5564 CA LEU 712 36.392 12.662 21.764 1.00 38.69 ATOM 5565 CB LEU 712 36.914 11.714 20.672 1.00 37.19 ATOM 5566 CG LEU 712 36.070 11.436 19.424 1.00 34.73 ATOM 5567 CD1 LEU 712 36.814 10.453 18.524 1.00 35.54 ATOM 5568 CD2 LEU 712 34.709 10.872 19.818 1.00 30.90 ATOM 5569 C LEU 712 37.230 12.472 23.021 1.00 39.62 ATOM 5570 O LEU 712 36.843 11.745 23.940 1.00 39.44 ATOM 5571 N LEU 713 38.398 13.101 23.044 1.00 40.10 ATOM 5573 CA LEU 713 39.279 12.999 24.199 1.00 42.81 ATOM 5574 CB LEU 713 40.606 13.736 23.924 1.00 41.70 ATOM 5575 CG LEU 713 41.495 13.040 22.868 1.00 41.86 ATOM 5576 CD1 LEU 713 42.742 13.862 22.607 1.00 37.19 ATOM 5577 CD2 LEU 713 41.873 11.647 23.340 1.00 41.17 ATOM 5578 C LEU 713 38.577 13.566 25.437 1.00 43.18 ATOM 5579 O LEU 713 38.479 12.889 26.457 1.00 44.79 ATOM 5580 N LYS 714 38.004 14.760 25.312 1.00 42.75 ATOM 5582 CA LYS 714 37.301 15.389 26.425 1.00 43.70 ATOM 5583 CB LYS 714 36.842 16.796 26.043 1.00 44.69 ATOM 5584 CG LYS 714 38.001 17.746 25.836 1.00 47.92 ATOM 5585 CD LYS 714 37.543 19.171 25.583 1.00 55.01 ATOM 5586 CE LYS 714 38.733 20.077 25.238 1.00 59.44 ATOM 5587 NZ LYS 714 39.773 20.132 26.320 1.00 60.10 ATOM 5591 C LYS 714 36.127 14.557 26.940 1.00 43.94 ATOM 5592 O LYS 714 35.843 14.551 28.140 1.00 44.20 ATOM 5593 N GLU 715 35.477 13.819 26.046 1.00 43.29 ATOM 5595 CA GLU 715 34.350 12.979 26.435 1.00 42.29 ATOM 5596 CB GLU 715 33.464 12.682 25.225 1.00 44.91 ATOM 5597 CG GLU 715 32.913 13.916 24.522 1.00 51.62 ATOM 5598 CD GLU 715 32.020 13.566 23.332 1.00 55.01 ATOM 5599 OD1 GLU 715 32.343 12.605 22.596 1.00 58.09 ATOM 5600 OE2 GLU 715 30.992 14.251 23.136 1.00 55.83 ATOM 5601 C GLU 715 34.806 11.665 27.064 1.00 41.07 ATOM 5602 O GLU 715 33.982 10.825 27.421 1.00 38.01 ATOM 5603 N GLY 716 36.118 11.476 27.182 1.00 41.11 ATOM 5605 CA GLY 716 36.642 10.252 27.770 1.00 39.69 ATOM 5606 C GLY 716 36.510 9.054 26.847 1.00 39.64 ATOM 5607 O GLY 716 36.562 7.904 27.290 1.00 36.71 ATOM 5608 N HIS 717 36.359 9.335 25.554 1.00 41.95 ATOM 5610 CA HIS 717 36.215 8.300 24.541 1.00 43.32 ATOM 5611 CB HIS 717 35.859 8.918 23.183 1.00 43.38 ATOM 5612 CG HIS 717 35.813 7.926 22.060 1.00 44.79 ATOM 5613 CD2 HIS 717 34.802 7.152 21.596 1.00 44.64 ATOM 5614 ND1 HIS 717 36.912 7.625 21.285 1.00 46.21 ATOM 5616 CE1 HIS 717 36.584 6.708 20.392 1.00 46.21 ATOM 5617 NE2 HIS 717 35.307 6.404 20.561 1.00 45.55 ATOM 5619 C HIS 717 37.485 7.481 24.403 1.00 43.90 ATOM 5620 O HIS 717 38.581 8.031 24.327 1.00 45.45 ATOM 5621 N ARG 718 37.304 6.169 24.289 1.00 43.44 ATOM 5623 CA ARG 718 38.387 5.207 24.139 1.00 42.68 ATOM 5624 CB ARG 718 38.500 4.361 25.412 1.00 41.00 ATOM 5625 CG ARG 718 38.844 5.165 26.658 1.00 40.09 ATOM 5626 CD ARG 718 40.214 5.825 26.495 1.00 41.06 ATOM 5627 NE ARG 718 40.658 6.549 27.685 1.00 39.51 ATOM 5629 CZ ARG 718 40.521 7.861 27.862 1.00 39.90 ATOM 5630 NH1 ARG 718 39.940 8.608 26.931 1.00 36.48 ATOM 5633 NH2 ARG 718 41.024 8.443 28.946 1.00 42.06 ATOM 5636 C ARG 718 38.080 4.308 22.927 1.00 43.91 ATOM 5637 O ARG 718 36.911 4.007 22.650 1.00 44.40 ATOM 5638 N MET 719 39.113 3.933 22.174 1.00 42.56 ATOM 5640 CA MET 719 38.928 3.079 21.004 1.00 42.82 ATOM 5641 CB MET 719 40.219 2.964 20.181 1.00 42.59 ATOM 5642 CG MET 719 40.595 4.221 19.413 1.00 41.15 ATOM 5643 SD MET 719 42.093 4.079 18.400 1.00 44.11 ATOM 5644 CE MET 719 43.323 3.949 19.613 1.00 41.33 ATOM 5645 C MET 719 38.460 1.694 21.432 1.00 44.74 ATOM 5646 O MET 719 38.822 1.216 22.516 1.00 41.56 ATOM 5647 N ASP 720 37.635 1.075 20.582 1.00 45.50 ATOM 5649 CA ASP 720 37.090 −0.265 20.824 1.00 45.51 ATOM 5650 CB ASP 720 36.077 −0.660 19.733 1.00 48.60 ATOM 5651 CG ASP 720 34.811 0.181 19.749 1.00 53.03 ATOM 5652 OD1 ASP 720 34.678 1.082 20.612 1.00 59.61 ATOM 5653 OD2 ASP 720 33.943 −0.067 18.880 1.00 50.58 ATOM 5654 C ASP 720 38.177 −1.329 20.823 1.00 43.64 ATOM 5655 O ASP 720 39.235 −1.172 20.199 1.00 43.66 ATOM 5656 N LYS 721 37.876 −2.436 21.487 1.00 42.90 ATOM 5658 CA LYS 721 38.784 −3.565 21.555 1.00 42.96 ATOM 5659 CB LYS 721 38.278 −4.565 22.587 1.00 42.51 ATOM 5660 CG LYS 721 39.000 −5.888 22.570 1.00 47.68 ATOM 5661 CD LYS 721 38.445 −6.805 23.628 1.00 51.61 ATOM 5662 CE LYS 721 38.450 −8.246 23.163 1.00 54.96 ATOM 5663 NZ LYS 721 38.165 −9.190 24.282 1.00 59.67 ATOM 5667 C LYS 721 38.825 −4.215 20.182 1.00 43.05 ATOM 5668 O LYS 721 37.779 −4.577 19.625 1.00 46.08 ATOM 5669 N PRO 722 40.025 −4.348 19.601 1.00 43.22 ATOM 5670 CD PRO 722 41.337 −3.672 20.067 1.00 43.52 ATOM 5671 CA PRO 722 40.139 −4.968 18.275 1.00 41.04 ATOM 5672 CB PRO 722 41.631 −4.856 17.965 1.00 40.87 ATOM 5673 CG PRO 722 42.074 −3.682 18.764 1.00 42.22 ATOM 5674 C PRO 722 39.726 −6.427 18.346 1.00 39.64 ATOM 5675 O PRO 722 39.730 −7.023 19.425 1.00 37.12 ATOM 5676 N SER 723 39.311 −6.982 17.212 1.00 40.36 ATOM 5678 CA SER 723 38.947 −8.389 17.158 1.00 41.41 ATOM 5679 CB SER 723 38.205 −8.707 15.865 1.00 38.26 ATOM 5680 OG SER 723 39.049 −8.520 14.749 1.00 43.87 ATOM 5682 C SER 723 40.294 −9.102 17.191 1.00 41.54 ATOM 5683 O SER 723 41.284 −8.575 16.703 1.00 40.90 ATOM 5684 N ASN 724 40.338 −10.300 17.750 1.00 44.89 ATOM 5686 CA ASN 724 41.598 −11.019 17.853 1.00 48.14 ATOM 5687 CB ASN 724 42.256 −11.202 16.476 1.00 52.43 ATOM 5688 CG ASN 724 41.682 −12.374 15.715 1.00 57.29 ATOM 5689 OD1 ASN 724 41.637 −13.492 16.225 1.00 61.96 ATOM 5690 ND2 ASN 724 41.218 −12.125 14.500 1.00 60.91 ATOM 5693 C ASN 724 42.509 −10.255 18.811 1.00 48.17 ATOM 5694 O ASN 724 43.648 −9.918 18.495 1.00 49.88 ATOM 5695 N CYS 725 41.960 −9.935 19.973 1.00 47.12 ATOM 5697 CA CYS 725 42.686 −9.238 21.010 1.00 46.17 ATOM 5698 CB CYS 725 42.569 −7.717 20.862 1.00 44.83 ATOM 5699 SG CYS 725 43.459 −6.813 22.159 1.00 42.51 ATOM 5700 C CYS 725 42.017 −9.697 22.294 1.00 45.78 ATOM 5701 O CYS 725 40.803 −9.642 22.423 1.00 44.83 ATOM 5702 N THR 726 42.810 −10.224 23.212 1.00 45.63 ATOM 5704 CA THR 726 42.289 −10.711 24.482 1.00 45.47 ATOM 5705 CB THR 726 43.351 −11.545 25.217 1.00 45.93 ATOM 5706 OG1 THR 726 44.307 −10.651 2S.786 1.00 45.04 ATOM 5708 CG2 THR 726 44.061 −12.495 24.233 1.00 42.99 ATOM 5709 C THR 726 41.858 −9.545 25.359 1.00 45.73 ATOM 5710 O THR 726 42.368 −8.445 25.216 1.00 46.91 ATOM 5711 N ASN 727 40.914 −9.789 26.257 1.00 45.93 ATOM 5713 CA ASN 727 40.448 −8.736 27.141 1.00 47.85 ATOM 5714 CB ASM 727 39.300 −9.237 28.022 1.00 54.88 ATOM 5715 CG ASN 727 39.629 −10.544 28.731 1.00 65.11 ATOM 5716 OD1 ASN 727 40.737 −10.734 29.229 1.00 70.58 ATOM 5717 ND2 ASN 727 38.681 −11.472 28.735 1.00 69.68 ATOM 5720 C ASN 727 41.591 −8.212 27.999 1.00 44.18 ATOM 5721 O ASN 727 41.594 −7.047 28.390 1.00 41.35 ATOM 5722 N GLU 728 42.572 −9.073 28.260 1.00 42.82 ATOM 5724 CA GLU 728 43.725 −8.713 29.071 1.00 42.37 ATOM 5725 CB GLU 728 44.573 −9.952 29.379 1.00 43.09 ATOM 5726 CG GLU 728 45.806 −9.654 30.245 1.00 48.30 ATOM 5727 CD GLU 728 46.643 −10.889 30.568 1.00 50.11 ATOM 5728 OE1 GLU 728 46.867 −11.732 29.668 1.00 47.98 ATOM 5729 OE2 GLU 728 47.085 −11.010 31.733 1.00 51.69 ATOM 5730 C GLU 728 44.551 −7.652 28.356 1.00 39.57 ATOM 5731 O GLU 728 44.852 −6.605 28.933 1.00 39.30 ATOM 5732 N LEU 729 44.872 −7.907 27.089 1.00 37.38 ATOM 5734 CA LEU 729 45.655 −6.977 26.274 1.00 36.74 ATOM 5735 CB LEU 729 46.027 −7.623 24.935 1.00 35.39 ATOM 5736 CG LEU 729 47.137 −8.679 25.001 1.00 35.41 ATOM 5737 CD1 LEU 729 47.107 −9.553 23.766 1.00 35.69 ATOM 5738 CD2 LEU 729 48.505 −8.017 25.174 1.00 37.72 ATOM 5739 C LEU 729 44.885 −5.679 26.050 1.00 35.52 ATOM 5740 O LEU 729 45.467 −4.597 25.941 1.00 33.96 ATOM 5741 N TYR 730 43.565 −5.779 26.000 1.00 32.90 ATOM 5743 CA TYR 730 42.760 −4.598 25.812 1.00 32.41 ATOM 5744 CB TYR 730 41.335 −4.981 25.398 1.00 32.16 ATOM 5745 CG TYR 730 40.445 −3.787 25.172 1.00 34.93 ATOM 5746 CD1 TYR 730 40.769 −2.827 24.203 1.00 32.49 ATOM 5747 CE1 TYR 730 39.962 −1.716 23.994 1.00 32.80 ATOM 5748 CD2 TYR 730 39.282 −3.605 25.931 1.00 33.45 ATOM 5749 CE2 TYR 730 38.465 −2.496 25.728 1.00 34.81 ATOM 5750 CZ TYR 730 38.814 −1.557 24.756 1.00 34.06 ATOM 5751 OH TYR 730 38.009 −0.465 24.551 1.00 36.66 ATOM 5753 C TYR 730 42.767 −3.788 27.107 1.00 33.48 ATOM 5754 O TYR 730 42.837 −2.558 27.083 1.00 34.94 ATOM 5755 N MET 731 42.698 −4.466 28.248 1.00 35.29 ATOM 5757 CA MET 731 42.724 −3.755 29.525 1.00 38.38 ATOM 5758 CB MET 731 42.465 −4.709 30.690 1.00 42.01 ATOM 5759 CG MET 731 41.048 −5.264 30.702 1.00 53.67 ATOM 5760 SD MET 731 39.785 −3.965 30.830 1.00 62.97 ATOM 5761 CE MET 731 39.828 −3.688 32.641 1.00 61.83 ATOM 5762 C MET 731 44.073 −3.049 29.670 1.00 34.52 ATOM 5763 O MET 731 44.160 −1.958 30.232 1.00 33.23 ATOM 5764 N MET 732 45.118 −3.669 29.134 1.00 33.93 ATOM 5766 CA MET 732 46.445 −3.065 29.168 1.00 36.26 ATOM 5767 CB MET 732 47.506 −3.995 28.565 1.00 35.56 ATOM 5768 CG MET 732 48.935 −3.418 28.643 1.00 35.26 ATOM 5769 SD MET 732 50.186 −4.522 28.001 1.00 30.46 ATOM 5770 CE MET 732 50.480 −5.562 29.415 1.00 26.88 ATOM 5771 C MET 732 46.369 −1.750 28.389 1.00 34.75 ATOM 5772 O MET 732 46.827 −0.722 28.873 1.00 35.49 ATOM 5773 N MET 733 45.741 −1.774 27.213 1.00 34.63 ATOM 5775 CA MET 733 45.571 −0.566 26.413 1.00 32.79 ATOM 5776 CB MET 733 44.787 −0.853 25.130 1.00 33.16 ATOM 5777 CG MET 733 45.544 −1.601 24.047 1.00 32.32 ATOM 5778 SD MET 733 44.421 −1.990 22.670 1.00 35.66 ATOM 5779 CE MET 733 45.155 −3.496 22.068 1.00 29.47 ATOM 5780 C MET 733 44.789 0.452 27.229 1.00 33.94 ATOM 5781 O MET 733 45.176 1.619 27.318 1.00 35.72 ATOM 5782 N ARG 734 43.679 0.018 27.818 1.00 33.73 ATOM 5784 CA ARG 734 42.854 0.913 28.621 1.00 33.41 ATOM 5785 CB ARG 734 41.586 0.197 29.095 1.00 33.42 ATOM 5786 CG ARG 734 40.726 −0.335 27.950 1.00 34.26 ATOM 5787 CD ARG 734 40.256 0.783 27.043 1.00 37.70 ATOM 5788 NE ARG 734 39.416 1.745 27.750 1.00 43.98 ATOM 5790 CZ ARG 734 38.092 1.661 27.844 1.00 46.43 ATOM 5791 NH1 ARG 734 37.439 0.660 27.268 1.00 48.63 ATOM 5794 NH2 ARG 734 37.420 2.571 28.530 1.00 44.65 ATOM 5797 C ARG 734 43.660 1.458 29.793 1.00 32.12 ATOM 5798 O ARG 734 43.492 2.610 30.180 1.00 35.37 ATOM 5799 N ASP 735 44.566 0.646 30.327 1.00 33.75 ATOM 5801 CA ASP 735 45.438 1.076 31.433 1.00 36.72 ATOM 5802 CB ASP 735 46.379 −0.055 31.857 1.00 42.71 ATOM 5803 CG ASP 735 45.722 −1.052 32.774 1.00 47.31 ATOM 5804 OD1 ASP 735 46.124 −2.241 32.720 1.00 50.99 ATOM 5805 OD2 ASP 735 44.824 −0.646 33.552 1.00 48.45 ATOM 5806 C ASP 735 46.291 2.251 30.972 1.00 34.25 ATOM 5807 O ASP 735 46.376 3.286 31.648 1.00 34.31 ATOM 5808 N CYS 736 46.927 2.064 29.816 1.00 31.85 ATOM 5810 CA CYS 736 47.780 3.077 29.204 1.00 29.93 ATOM 5811 CB CYS 736 48.413 2.545 27.921 1.00 24.97 ATOM 5812 SG CYS 736 49.504 1.159 28.180 1.00 31.35 ATOM 5813 C CYS 736 46.994 4.325 28.885 1.00 31.62 ATOM 5814 O CYS 736 47.562 5.416 28.823 1.00 30.73 ATOM 5815 N TRP 737 45.680 4.174 28.711 1.00 35.03 ATOM 5817 CA TRP 737 44.812 5.308 28.395 1.00 36.35 ATOM 5818 CB TRP 737 43.808 4.927 27.297 1.00 36.43 ATOM 5819 CG TRP 737 44.451 4.487 26.0:0 1.00 34.34 ATOM 5820 CD2 TRP 737 43.914 3.565 25.052 1.00 34.81 ATOM 5821 CE2 TRP 737 44.852 3.461 23.999 1.00 33.92 ATOM 5822 CE3 TRP 737 42.730 2.816 24.980 1.00 33.06 ATOM 5823 CD1 TRP 737 45.659 4.890 25.514 1.00 35.19 ATOM 5824 NE1 TRP 737 45.907 4.279 24.309 1.00 35.00 ATOM 5826 CZ2 TRP 737 44.644 2.633 22.886 1.00 33.45 ATOM 5827 CZ3 TRP 737 42.527 1.991 23.876 1.00 32.92 ATOM 5828 CH2 TRP 737 43.480 1.909 22.844 1.00 30.45 ATOM 5829 C TRP 737 44.080 5.895 29.609 1.00 37.23 ATOM 5830 O TRP 737 43.047 6.551 29.474 1.00 37.44 ATOM 5831 N HIS 738 44.624 5.681 30.798 1.00 41.45 ATOM 5833 CA HIS 738 44.006 6.208 32.008 1.00 41.52 ATOM 5834 CB HIS 738 44.675 5.635 33.258 1.00 41.23 ATOM 5835 CG HIS 738 43.925 5.924 34.522 1.00 43.31 ATOM 5836 CD2 HIS 738 43.618 7.096 35.126 1.00 41.58 ATOM 5837 ND1 HIS 738 43.338 4.935 35.279 1.00 44.22 ATOM 5839 CE1 HIS 738 42.693 5.487 36.294 1.00 46.62 ATOM 5840 NE2 HIS 738 42.848 6.798 36.223 1.00 43.99 ATOM 5842 C HIS 738 44.118 7.726 32.015 1.00 41.75 ATOM 5843 O HIS 738 45.179 8.268 31.731 1.00 40.84 ATOM 5844 N ALA 739 43.025 8.405 32.352 1.00 42.47 ATOM 5846 CA ALA 739 43.004 9.873 32.398 1.00 44.58 ATOM 5847 CB ALA 739 41.629 10.361 32.825 1.00 48.19 ATOM 5848 C ALA 739 44.081 10.467 33.317 1.00 45.12 ATOM 5849 O ALA 739 44.653 11.510 33.020 1.00 45.66 ATOM 5850 N VAL 740 44.262 9.852 34.481 1.00 46.64 ATOM 5852 CA VAL 740 45.278 10.273 35.453 1.00 46.78 ATOM 5853 CB VAL 740 44.867 9.893 36.888 1.00 47.74 ATOM 5854 CG1 VAL 740 45.919 10.372 37.890 1.00 49.35 ATOM 5855 CG2 VAL 740 43.515 10.495 37.211 1.00 47.89 ATOM 5856 C VAL 740 46.601 9.573 35.121 1.00 45.24 ATOM 5857 O VAL 740 46.754 8.362 35.347 1.00 45.01 ATOM 5858 N PRO 741 47.588 10.335 34.637 1.00 43.46 ATOM 5859 CD PRO 741 47.536 11.794 34.437 1.00 43.51 ATOM 5860 CA PRO 741 48.905 9.804 34.266 1.00 46.22 ATOM 5861 CS PRO 741 49.701 11.070 33.942 1.00 45.32 ATOM 5862 CG PRO 741 48.632 12.010 33.426 1.00 42.81 ATOM 5863 C PRO 741 49.588 8.936 35.328 1.00 47.45 ATOM 5864 O PRO 741 50.245 7.950 34.994 1.00 45.12 ATOM 5865 N SER 742 49.394 9.280 36.601 1.00 48.78 ATOM 5867 CA SER 742 49.994 8.532 37.703 1.00 48.76 ATOM 5868 CB SER 742 49.845 9.317 39.012 1.00 51.11 ATOM 5869 OG SER 742 48.482 9.488 39.373 1.00 53.50 ATOM 5871 C SER 742 49.376 7.150 37.867 1.00 47.77 ATOM 5872 O SER 742 49.932 6.283 38.539 1.00 47.31 ATOM 5873 N GLN 743 48.199 6.962 37.284 1.00 47.57 ATOM 5875 CA GLN 743 47.511 5.689 37.384 1.00 47.14 ATOM 5876 CB GLN 743 46.004 5.918 37.531 1.00 50.16 ATOM 5877 CG GLN 743 45.438 5.447 38.671 1.00 54.69 ATOM 5878 CD GLN 743 46.239 5.964 40.051 1.00 57.62 ATOM 5879 OE1 GLN 743 46.898 5.196 40.749 1.00 59.09 ATOM 5880 NE2 GLN 743 46.202 7.277 40.268 1.00 59.45 ATOM 5883 C GLN 743 47.816 4.774 36.212 1.00 44.41 ATOM 5884 O GLN 743 47.365 3.627 36.182 1.00 44.39 ATOM 5885 N ARG 744 48.515 5.305 35.212 1.00 42.87 ATOM 5887 CA ARG 744 48.902 4.506 34.046 1.00 41.45 ATOM 5888 CB ARG 744 49.350 5.397 32.883 1.00 37.34 ATOM 5889 CG ARG 744 48.316 6.380 32.412 1.00 32.30 ATOM 5890 CD ARG 744 48.854 7.207 31.270 1.00 31.37 ATOM 5891 NE ARG 744 47.921 8.276 30.946 1.00 36.76 ATOM 5893 CZ ARG 744 48.271 9.492 30.543 1.00 39.88 ATOM 5894 NH1 ARG 744 49.553 9.813 30.399 1.00 39.94 ATOM 5897 NH2 ARG 744 47.330 10.404 30.322 1.00 39.12 ATOM 5900 C ARG 744 50.068 3.616 34.471 1.00 41.40 ATOM 5901 O ARG 744 50.813 3.945 35.405 1.00 42.84 ATOM 5902 N PRO 745 50.203 2.441 33.849 1.00 40.11 ATOM 5903 CD PRO 745 49.245 1.739 32.876 1.00 39.91 ATOM 5904 CA PRO 745 51.332 1.607 34.266 1.00 38.58 ATOM 5905 CB PRO 745 51.019 0.261 33.605 1.00 37.46 ATOM 5906 CG PRO 745 50.250 0.645 32.377 1.00 37.41 ATOM 5907 C PRO 745 52.640 2.202 33.750 1.00 37.73 ATOM 5908 O PRO 745 52.634 3.027 32.835 1.00 37.71 ATOM 5909 N THR 746 53.753 1.843 34.373 1.00 35.90 ATOM 5911 CA THR 746 55.050 2.328 33.913 1.00 34.77 ATOM 5912 CB THR 746 56.085 2.380 35.075 1.00 33.85 ATOM 5913 OG1 THR 746 56.296 1.059 35.602 1.00 33.92 ATOM 5915 CG2 THR 746 55.605 3.302 36.177 1.00 32.17 ATOM 5916 C THR 746 55.544 1.327 32.870 1.00 32.69 ATOM 5917 O THR 746 55.026 0.213 32.795 1.00 31.56 ATOM 5918 N PHE 747 56.538 1.708 32.066 1.00 34.04 ATOM 5920 CA PHE 747 57.093 0.782 31.083 1.00 31.74 ATOM 5921 CB PHE 747 58.121 1.472 30.193 1.00 30.55 ATOM 5922 CG PHE 747 57.504 2.287 29.096 1.00 29.40 ATOM 5923 CD1 PHE 747 56.772 1.666 28.092 1.00 28.24 ATOM 5924 CD2 PHE 747 57.609 3.667 29.091 1.00 27.50 ATOM 5925 CE1 PHE 747 56.170 2.407 27.100 1.00 24.35 ATOM 5926 CE2 PHE 747 57.001 4.413 28.091 1.00 29.27 ATOM 5927 CZ PHE 747 56.276 3.776 27.103 1.00 25.73 ATOM 5928 C PHE 747 57.714 −0.413 31.782 1.00 31.92 ATOM 5929 O PHE 747 57.727 −1.514 31.243 1.00 32.46 ATOM 5930 N LYS 748 58.233 −0.199 32.986 1.00 33.47 ATOM 5932 CA LYS 748 58.816 −1.302 33.733 1.00 35.57 ATOM 5933 CB LYS 748 59.468 −0.800 35.026 1.00 39.42 ATOM 5934 CG LYS 748 60.083 −1.923 35.861 1.00 46.49 ATOM 5935 CD LYS 748 60.817 −1.407 37.103 1.00 50.69 ATOM 5936 CE LYS 748 61.253 −2.574 37.999 1.00 52.57 ATOM 5937 NE LYS 748 62.072 −2.129 39.155 1.00 56.45 ATOM 5941 C LYS 748 57.700 −2.318 34.028 1.00 35.58 ATOM 5942 O LYS 748 57.898 −3.526 33.871 1.00 34.72 ATOM 5943 N GLN 749 56.522 −1.818 34.411 1.00 35.59 ATOM 5945 CA GLN 749 55.369 −2.684 34.692 1.00 38.20 ATOM 5946 CB GLN 749 54.154 −1.872 35.162 1.00 42.73 ATOM 5947 CG GLN 749 54.264 −1.171 36.499 1.00 49.30 ATOM 5948 CD GLN 749 53.060 −0.282 36.761 1.00 53.13 ATOM 5949 OE1 GLN 749 53.194 −0.915 37.023 1.00 52.71 ATOM 5950 NE2 GLN 749 51.873 −0.856 36.644 1.00 58.54 ATOM 5953 C GLN 749 54.954 −3.392 33.409 1.00 36.16 ATOM 5954 O GLN 749 54.745 −4.605 33.393 1.00 36.67 ATOM 5955 N LEU 750 54.801 −2.609 32.342 1.00 35.83 ATOM 5957 CA LEU 750 54.381 −3.117 31.037 1.00 34.49 ATOM 5958 CB LEU 750 54.324 −1.988 30.004 1.00 32.49 ATOM 5959 CG LEU 750 53.206 −0.958 30.188 1.00 31.94 ATOM 5960 CD1 LEU 750 53.411 −0.230 29.267 1.00 30.45 ATOM 5961 CD2 LEU 750 51.859 −1.610 29.933 1.00 29.30 ATOM 5962 C LEU 750 55.294 −4.214 30.559 1.00 33.87 ATOM 5963 O LEU 750 54.828 −5.208 30.027 1.00 34.72 ATOM 5964 N VAL 751 56.598 −4.038 30.759 1.00 36.12 ATOM 5966 CA VAL 751 57.585 −5.045 30.363 1.00 34.50 ATOM 5967 CB VAL 751 59.054 −4.532 30.559 1.00 31.96 ATOM 5968 CG1 VAL 751 60.052 −5.646 30.308 1.00 30.24 ATOM 5969 CG2 VAL 751 59.342 −3.386 29.604 1.00 28.02 ATOM 5970 C VAL 751 57.349 −6.321 31.182 1.00 36.11 ATOM 5971 O VAL 751 57.333 −7.422 30.638 1.00 36.45 ATOM 5972 N GLU 752 57.107 −6.165 32.479 1.00 37.83 ATOM 5974 CA GLU 752 56.869 −7.326 33.331 1.00 41.47 ATOM 5975 CB GLU 752 56.800 −6.919 34.804 1.00 43.03 ATOM 5976 CG GLU 752 58.122 −6.305 35.263 1.00 52.52 ATOM 5977 CD GLU 752 58.251 −6.176 36.761 1.00 57.18 ATOM 5978 OE1 GLU 752 58.600 −5.068 37.233 1.00 58.11 ATOM 5979 OE2 GLU 752 58.032 −7.191 37.461 1.00 61.59 ATOM 5980 C GLU 752 55.623 −8.097 32.890 1.00 40.16 ATOM 5981 O GLU 752 55.689 −9.308 32.642 1.00 39.75 ATOM 5982 N ASP 753 54.524 −7.376 32.696 1.00 40.06 ATOM 5984 CA ASP 753 53.275 −7.982 32.264 1.00 39.73 ATOM 5985 CB ASP 753 52.157 −6.947 32.247 1.00 41.00 ATOM 5986 CG ASP 753 51.668 −6.591 33.640 1.00 45.17 ATOM 5987 OD1 ASP 753 51.753 −7.468 34.543 1.00 49.78 ATOM 5988 OD2 ASP 753 51.210 −5.439 33.829 1.00 45.51 ATOM 5989 C ASP 753 53.396 −8.595 30.890 1.00 39.64 ATOM 5990 O ASP 753 52.955 −9.720 30.674 1.00 41.84 ATOM 5991 N LEU 754 53.998 −7.861 29.960 1.00 37.75 ATOM 5993 CA LEU 754 54.161 −8.358 28.603 1.00 38.16 ATOM 5994 CB LEU 754 54.664 −7.261 27.664 1.00 36.95 ATOM 5995 CG LEU 754 53.552 −6.270 27.307 1.00 36.64 ATOM 5996 CD1 LEU 754 54.141 −5.062 26.590 1.00 34.02 ATOM 5997 CD2 LEU 754 52.459 −6.968 26.465 1.00 34.13 ATOM 5998 C LEU 754 55.070 −9.561 28.571 1.00 38.46 ATOM 5999 O LEU 754 54.905 −10.451 27.740 1.00 39.95 ATOM 6000 N ASP 755 56.014 −9.602 29.502 1.00 39.19 ATOM 6002 CA ASP 755 56.930 −10.728 29.594 1.00 40.87 ATOM 6003 CB ASP 755 57.956 −10.462 30.696 1.00 45.11 ATOM 6004 CG ASP 755 59.128 −11.415 30.652 1.00 48.64 ATOM 6005 OD1 ASP 755 59.759 −11.612 31.711 1.00 54.27 ATOM 6006 OD2 ASP 755 59.432 −11.954 29.565 1.00 51.46 ATOM 6007 C ASP 755 56.082 −11.952 29.947 1.00 40.67 ATOM 6008 O ASP 755 56.152 −12.996 29.289 1.00 38.49 ATOM 6009 N ARG 756 55.232 −11.771 30.955 1.00 40.06 ATOM 6011 CA ARG 756 54.340 −12.817 31.437 1.00 40.07 ATOM 6012 CB ARG 756 53.573 −12.316 32.661 1.00 40.24 ATOM 6013 CG ARG 756 52.435 −13.217 33.138 1.00 42.12 ATOM 6014 CD ARG 756 51.791 −12.631 34.389 1.00 42.33 ATOM 6015 NE ARG 756 51.353 −12.247 34.186 1.00 46.68 ATOM 6017 CZ ARG 756 50.295 −10.891 33.460 1.00 48.17 ATOM 6018 NH1 ARG 756 49.549 −11.818 32.866 1.00 46.64 ATOM 6021 NH2 ARG 756 49.998 −9.605 33.305 1.00 48.92 ATOM 6024 C ARG 756 53.362 −13.275 30.364 1.00 40.19 ATOM 6025 O ARG 756 53.247 −14.469 30.110 1.00 42.24 ATOM 6026 N ILE 757 52.688 −12.327 29.717 1.00 38.18 ATOM 6028 CA ILE 757 51.706 −12.649 28.683 1.00 38.40 ATOM 6029 CB ILE 757 50.952 −11.382 28.187 1.00 36.55 ATOM 6030 CG2 ILE 757 49.952 −11.758 27.105 1.00 34.67 ATOM 6031 CG1 ILE 757 50.216 −10.726 29.364 1.00 34.65 ATOM 6032 CD1 ILE 757 49.554 −9.423 29.048 1.00 36.49 ATOM 6033 C ILE 757 52.301 −13.400 27.500 1.00 39.19 ATOM 6034 O ILE 757 51.709 −14.360 27.025 1.00 39.66 ATOM 6035 N VAL 758 53.492 −12.996 27.061 1.00 42.36 ATOM 6037 CA VAL 758 54.161 −13.645 25.937 1.00 43.15 ATOM 6038 CB VAL 758 55.582 −13.052 25.682 1.00 41.72 ATOM 6039 CG1 VAL 758 56.308 −13.855 24.621 1.00 41.57 ATOM 6040 CG2 VAL 758 55.491 −11.619 25.229 1.00 40.06 ATOM 6041 C VAL 758 54.299 −15.133 26.231 1.00 47.11 ATOM 6042 O VAL 758 54.045 −15.971 25.369 1.00 48.62 ATOM 6043 N ALA 759 54.695 −15.446 27.464 1.00 49.64 ATOM 6045 CA ALA 759 54.879 −16.820 27.908 1.00 51.35 ATOM 6046 CB ALA 759 55.423 −16.830 29.317 1.00 50.11 ATOM 6047 C ALA 759 53.568 −17.598 27.850 1.00 54.72 ATOM 6048 O ALA 759 53.520 −18.717 27.348 1.00 58.64 ATOM 6049 N LEU 760 52.496 −16.983 28.329 1.00 54.84 ATOM 6051 CA LEU 760 51.194 −17.628 28.343 1.00 55.87 ATOM 6052 CB LEU 760 50.330 −17.034 29.459 1.00 56.85 ATOM 6053 CG LEU 760 50.875 −17.165 30.885 1.00 56.80 ATOM 6054 CD1 LEU 760 49.991 −16.392 31.849 1.00 56.78 ATOM 6055 CD2 LEU 760 50.959 −18.631 31.289 1.00 57.78 ATOM 6056 C LEU 760 50.454 −17.546 27.013 1.00 57.36 ATOM 6057 O LEU 760 49.262 −17.859 26.944 1.00 57.65 ATOM 6058 N THR 761 51.151 −17.134 25.956 1.00 58.71 ATOM 6060 CA THR 761 50.541 −17.025 24.630 1.00 59.04 ATOM 6061 CB THR 761 50.839 −15.657 23.971 1.00 56.72 ATOM 6062 OG1 THR 761 50.287 −14.610 24.775 1.00 56.53 ATOM 6064 CG2 THR 761 50.213 −15.584 22.590 1.00 53.81 ATOM 6065 C THR 761 51.049 −13.138 23.721 1.00 60.44 ATOM 6066 O THR 761 52.255 −18.295 23.530 1.00 61.40 ATOM 6067 SG CYS 1603 18.474 −8.976 20.202 0.50 37.82 PRT2 ATOM 6068 CG MET 534 69.311 12.109 23.281 0.50 36.25 PRT2 ATOM 6069 SD MET 534 69.286 12.958 24.867 0.50 42.66 PRT2 ATOM 6070 CE MET 534 70.539 12.082 25.804 0.50 43.27 PRT2 ATOM 6071 SG CYS 603 56.046 −7.949 16.446 0.50 36.47 PRT2 ATOM 2676 OH2 TIP3 1 71.794 25.061 2.660 1.00 24.53 ATOM 2679 OH2 TIP3 2 39.750 3.992 15.898 1.00 39.62 ATOM 2682 OH2 TIP3 3 83.809 19.717 10.596 1.00 28.26 ATOM 2685 OH2 TIP3 4 83.630 20.056 7.685 1.00 26.19 ATOM 2688 OH2 TIP3 5 75.073 16.616 6.785 1.00 26.48 ATOM 2691 OH2 TIP3 6 86.549 19.594 9.502 1.00 33.65 ATOM 2694 OH2 TIP3 7 51.913 11.060 24.263 1.00 35.55 ATOM 2697 OH2 TIP3 8 55.093 9.421 22.524 1.00 26.63 ATOM 2700 OH2 TIP3 9 57.161 4.614 32.443 1.00 29.69 ATOM 2703 OH2 TIP3 10 52.169 4.735 13.281 1.00 22.61 ATOM 2706 OH2 TIP3 11 41.110 5.543 22.764 1.00 41.60 ATOM 2709 OH2 TIP3 12 45.145 8.857 21.555 1.00 36.99 ATOM 2712 OH2 TIP3 13 64.465 −2.607 28.883 1.00 30.17 ATOM 2715 OH2 TIP3 14 76.944 13.287 23.954 1.00 32.94 ATOM 2718 OH2 TIP3 15 79.062 17.048 18.200 1.00 51.65 ATOM 2721 OH2 TIP3 16 83.066 11.657 15.958 1.00 25.12 ATOM 2724 OH2 TIP3 17 13.957 −9.951 0.095 1.00 26.02 ATOM 2727 OH2 TIP3 18 38.359 −0.001 5.000 1.00 37.43 ATOM 2730 OH2 TIP3 19 5.442 2.705 19.077 1.00 29.46 ATOM 2733 OH2 TIP3 20 27.008 6.166 4.885 1.00 25.05 ATOM 2736 OH2 TIP3 21 34.242 −1.725 16.911 1.00 52.12 ATOM 2739 OH2 TIP3 22 20.167 2.428 27.681 1.00 42.69 ATOM 2742 OH2 TIP3 23 50.794 −11.834 38.045 1.00 60.16 ATOM 2745 OH2 TIP3 24 17.261 −5.993 −1.757 1.00 25.88 ATOM 2748 OH2 TIP3 25 27.516 7.803 15.070 1.00 39.33 ATOM 2751 OH2 TIP3 26 31.574 0.146 6.684 1.00 35.78 ATOM 2754 OH2 TIP3 27 27.119 −12.972 27.844 1.00 43.66 ATOM 2757 OH2 TIP3 28 28.439 −17.074 13.203 1.00 36.44 ATOM 2760 OH2 TIP3 29 88.706 14.393 7.969 1.00 32.49 ATOM 2763 OH2 TIP3 30 −2.338 −3.424 11.295 1.00 49.20 ATOM 2766 0H2 TIP3 31 35.086 −4.130 18.836 1.00 37.83 ATOM 2769 OH2 TIP3 32 80.455 17.922 9.507 1.00 23.69 ATOM 2772 OH2 TIP3 33 5.538 3.619 10.835 1.00 29.13 ATOM 2775 OH2 TIP3 34 −10.685 5.290 11.288 1.00 24.40 ATOM 2778 OH2 TIP3 35 29.210 −8.799 20.241 1.00 46.52 ATOM 2781 OH2 TIP3 36 6.195 3.150 13.803 1.00 31.39 ATOM 2784 OH2 TIP3 37 31.898 2.830 0.154 1.00 40.17 ATOM 2787 OH2 TIP3 38 19.915 2.023 −3.939 1.00 31.34 ATOM 2790 OH2 TIP3 39 62.242 2.604 32.859 1.00 39.67 ATOM 2793 OH2 TIP3 40 21.231 −7.063 −3.900 1.00 23.55 ATOM 2796 OH2 TIP3 41 −15.809 8.838 22.610 1.00 36.02 ATOM 2799 OH2 TIP3 42 40.120 2.154 8.433 1.00 60.62 ATOM 2802 OH2 TIP3 43 19.583 11.128 −0.045 1.00 37.85 ATOM 2805 OH2 TIP3 44 67.056 9.030 17.389 1.00 29.79 ATOM 2808 OH2 TIP3 45 87.772 18.919 18.595 1.00 48.44 ATOM 2811 OH2 TIP3 46 74.584 17.123 4.200 1.00 39.18 ATOM 2814 OH2 TIP3 47 29.365 16.707 10.560 1.00 34.11 ATOM 2817 OH2 TIP3 48 66.486 6.826 15.051 1.00 32.28 ATOM 2820 OH2 TIP3 49 85.008 21.441 5.731 1.00 23.97 ATOM 2823 OH2 TIP3 50 −4.572 2.912 3.173 1.00 28.05 ATOM 2826 OH2 TIP3 51 19.496 5.141 4.881 1.00 28.88 ATOM 2829 OH2 TIP3 52 67.492 3.490 10.902 1.00 33.57 ATOM 2832 OH2 TIP3 53 34.791 5.413 24.797 1.00 40.16 ATOM 2835 OH2 TIP3 54 34.787 −16.910 13.756 1.00 39.46 ATOM 2838 OH2 TIP3 55 59.972 7.450 27.870 1.00 31.56 ATOM 2841 OH2 TIP3 56 −7.139 −1.696 6.345 1.00 42.00 ATOM 2844 OH2 TIP3 57 54.998 11.953 25.360 1.00 42.05 ATOM 2847 OH2 TIP3 58 68.697 6.686 16.740 1.00 46.12 ATOM 2850 OH2 TIP3 59 73.750 20.885 19.041 1.00 32.26 ATOM 2853 OH2 TIP3 60 3.431 −8.270 −8.218 1.00 31.22 ATOM 2856 OH2 TIP3 61 37.904 10.790 5.612 1.00 33.72 ATOM 2859 OH2 TIP3 62 29.982 −9.545 −1.303 1.00 39.11 ATOM 2862 OH2 TIP3 63 66.918 1.757 8.678 1.00 34.68 ATOM 2865 OH2 TIP3 64 49.117 1.310 12.227 1.00 34.31 ATON 2868 OH2 TIP3 65 41.246 3.987 29.033 1.00 34.55 ATOM 2871 OH2 TIP3 66 10.755 −12.957 1.167 1.00 42.14 ATOM 2874 OH2 TIP3 67 −1.184 −4.327 21.439 1.00 37.90 ATOM 2877 OH2 TIP3 68 30.349 16.267 13.265 1.00 55.23 ATOM 2880 OH2 TIP3 69 8.111 4.362 3.445 1.00 23.88 ATOM 2883 OH2 TIP3 70 73.131 18.780 22.628 1.00 40.20 ATOM 2886 OH2 TIP3 71 −7.949 −3.409 24.953 1.00 35.49 ATOM 2889 OH2 TIP3 72 66.379 −4.621 28.423 1.00 45.46 ATOM 2892 OH2 TIP3 73 21.506 −20.711 4.815 1.00 52.46 ATOM 2895 OH2 TIP3 74 59.539 −6.865 4.928 1.00 48.87 ATOM 2898 OH2 TIP3 75 16.565 −13.297 −3.008 1.00 51.80 ATOM 2901 OH2 TIP3 76 −15.235 7.385 4.428 1.00 29.13 ATOM 2904 OH2 TIP3 77 32.926 2.785 13.213 1.00 37.62 ATOM 2907 OH2 TIP3 78 0.246 −2.768 10.996 1.00 28.25 ATOM 2910 OH2 TIP3 79 17.495 2.354 5.447 1.00 23.63 ATOM 2913 OH2 TIP3 80 6.336 2.434 21.950 1.00 29.56 ATOM 2916 OH2 TIP3 81 27.374 3.628 6.163 1.00 34.06 ATOM 2919 OH2 TIP3 82 −8.708 6.263 9.522 1.00 30.34 ATOM 2922 OH2 TIP3 83 1.500 −1.935 8.721 1.00 27.61 ATOM 2925 OH2 TIP3 84 −4.825 −3.133 6.984 1.00 33.50 ATOM 2928 OH2 TIP3 85 17.513 2.839 1.966 1.00 24.27 ATOM 2931 OH2 TIP3 86 20.298 3.414 2.920 1.00 26.15 ATOM 2934 OH2 TIP3 87 0.488 −2.158 22.213 1.00 25.95 ATOM 2937 OH2 TIP3 88 19.939 −6.185 −1.553 1.00 19.14 ATOM 2940 OH2 TIP3 89 10.670 −15.654 6.839 1.00 33.36 ATOM 2943 OH2 TIP3 90 4.107 −12.003 11.805 1.00 33.92 ATOM 2946 OH2 TIP3 91 6.238 0.927 −3.342 1.00 23.31 ATOM 2949 OH2 TIP3 92 −13.563 1.438 5.472 1.00 27.86 ATOM 2952 OH2 TIP3 93 15.707 −7.454 0.106 1.00 26.69 ATOM 2955 OH2 TIP3 94 −1.856 −5.393 3.795 1.00 39.91 ATOM 2958 OH2 TIP3 95 12.654 4.928 −4.474 1.00 31.32 ATOM 2961 OH2 TIP3 96 69.774 27.363 2.127 1.00 35.86 ATOM 2964 OH2 TIP3 97 24.636 −13.192 0.040 1.00 48.53 ATOM 2967 OH2 TIP3 98 60.453 −4.625 33.829 1.00 31.97 ATOM 2970 OH2 TIP3 99 10.513 5.719 3.487 1.00 38.90 ATOM 2973 OH2 TIP3 100 −9.499 −4.011 4.342 1.00 30.61 ATOM 2976 OH2 TIP3 101 73.056 −1.608 10.514 1.00 36.08 ATOM 2979 OH2 TIP3 102 −3.152 5.709 30.608 1.00 29.38 ATOM 2982 OH2 TIP3 103 36.630 0.702 11.792 1.00 47.80 ATOM 2985 OH2 TIP3 104 21.475 6.325 16.924 1.00 24.03 ATOM 2988 OH2 TIP3 105 31.272 0.656 19.432 1.00 53.74 ATOM 2991 OH2 TIP3 106 5.620 −8.417 22.266 1.00 51.90 ATOM 2994 OH2 TIP3 107 −13.144 8.294 17.464 1.00 35.23 ATOM 2997 OH2 TIP3 108 26.680 −10.556 −1.042 1.00 27.83 ATOM 3000 OH2 TIP3 109 24.149 1.846 18.172 1.00 30.90 ATOM 3003 OH2 TIP3 110 −1.943 12.643 3.558 1.00 33.82 ATOM 3006 OH2 TIP3 111 59.560 13.617 33.196 1.00 54.79 ATOM 3009 OH2 TIP3 112 4.351 −10.740 1.991 1.00 37.96 ATOM 3012 OH2 TIP3 113 8.396 2.913 0.958 1.00 29.64 ATOM 3015 OH2 TIP3 114 75.905 1.753 25.812 1.00 38.73 ATOM 3018 OH2 TIP3 115 48.783 15.535 14.189 1.00 35.24 ATOM 3021 OH2 TIP3 116 2.419 −11.312 9.146 1.00 32.85 ATOM 3024 OH2 TIP3 117 83.014 26.360 12.964 1.00 41.83 ATOM 3027 OH2 TIP3 118 8.761 −6.579 −3.252 1.00 42.78 ATOM 3030 OH2 TIP3 119 −8.417 4.493 4.305 1.00 28.32 ATOM 3033 OH2 TIP3 120 7.908 −13.690 8.639 1.00 33.73 ATOM 3036 OH2 TIP3 121 51.437 6.329 10.373 1.00 31.72 ATOM 3039 OH2 TIP3 122 20.660 3.686 15.591 1.00 32.31 ATOM 3042 OH2 TIP3 123 73.039 3.790 20.450 1.00 35.80 ATOM 3045 OH2 TIP3 124 5.155 −11.467 22.590 1.00 45.12 ATOM 3048 OH2 TIP3 125 34.172 2.412 16.576 1.00 41.90 ATOM 3051 OH2 TIP3 126 9.597 −11.905 7.083 1.00 24.83 ATOM 3054 OH2 TIP3 127 8.276 3.860 −1.622 1.00 35.46 ATOM 3057 OH2 TIP3 128 66.282 5.755 12.352 1.00 35.43 ATOM 3060 OH2 TIP3 129 7.377 6.932 2.982 1.00 40.68 ATOM 3063 OH2 TIP3 130 35.832 −1.778 0.201 1.00 34.99 ATOM 3066 OH2 TIP3 131 44.781 10.362 11.064 1.00 42.31 ATOM 3069 OH2 TIP3 132 27.790 −12.638 18.958 1.00 58.71 ATOM 3072 OH2 TIP3 133 45.221 11.540 21.428 1.00 36.75 ATOM 3075 OH2 TIP3 134 57.560 −10.846 14.099 1.00 52.90 ATOM 3078 OH2 TIP3 135 −3.354 15.001 16.515 1.00 37.81 ATOM 3081 OH2 TIP3 136 85.717 11.251 9.062 1.00 35.18 ATOM 3084 OH2 TIP3 137 12.951 −2.469 2.075 1.00 22.07 ATOM 3087 OH2 TIP3 138 75.645 3.486 20.527 1.00 38.01 ATOM 3090 OH2 TIP3 139 13.237 7.412 −2.649 1.00 33.50 ATOM 3093 OH2 TIP3 140 11.262 −9.970 0.974 1.00 26.14 ATOM 3096 OH2 TIP3 141 59.480 10.772 14.098 1.00 52.08 ATOM 3099 OH2 TIP3 142 13.869 −16.121 3.919 1.00 40.06 ATOM 3102 OH2 TIP3 143 −6.407 −3.413 16.641 1.00 44.38 ATOM 3105 OH2 TIP3 144 25.667 −12.645 3.411 1.00 48.28 ATOM 3108 OH2 TIP3 145 −16.282 10.641 6.423 1.00 40.94 ATOM 3111 OH2 TIP3 146 86.637 12.861 7.008 1.00 39.45 ATOM 3114 OH2 TIP3 147 32.082 −4.569 1.892 1.00 27.35 ATOM 3117 OH2 TIP3 148 44.809 7.627 11.670 1.00 35.65 ATOM 3120 OH2 TIP3 149 80.693 12.459 16.523 1.00 37.21 ATOM 3123 OH2 TIP3 150 2.941 −7.118 −1.805 1.00 38.43 ATOM 3126 OH2 TIP3 151 31.794 −6.086 20.704 1.00 42.80 ATOM 3129 OH2 TIP3 152 74.770 −2.683 12.398 1.00 40.40 ATOM 3132 OH2 TIP3 153 7.731 6.640 −1.037 1.00 35.61 ATOM 3135 OH2 TIP3 154 71.617 5.599 21.838 1.00 40.14 ATOM 3138 OH2 TIP3 155 68.113 −4.968 8.886 1.00 34.38 ATOM 3141 OH2 TIP3 156 0.042 −9.364 7.055 1.00 33.08 ATOM 3144 OH7 TIP3 157 68.020 18.352 10.995 1.00 34.76 ATOM 3147 OH2 TIP3 158 3.795 8.550 4.533 1.00 34.69 ATOM 3150 OH2 TIP3 159 52.106 11.746 18.410 1.00 40.06 ATOM 3153 OH2 TIP3 160 6.414 3.927 16.889 1.00 37.07 ATOM 3156 OH2 TIP3 161 −10.282 6.603 4.715 1.00 38.48 ATOM 3159 OH2 TIP3 162 76.410 1.681 −0.781 1.00 42.87 ATOM 3162 OH2 TIP3 163 9.910 −12.046 17.157 1.00 32.79 ATOM 3165 OH2 TIP3 164 33.983 14.219 18.191 1.00 37.35 ATOM 3168 OH2 TIP3 165 2.330 −7.952 16.978 1.00 44.25 ATOM 3171 OH2 TIP3 166 29.701 1.780 5.987 1.00 39.86 ATOM 3174 OH2 TIP3 167 32.494 −17.319 11.798 1.00 38.46 ATOM 3177 OH2 TIP3 168 42.107 17.932 10.978 1.00 44.83 ATOM 3180 OH2 TIP3 169 87.822 10.537 5.568 1.00 54.30 ATOM 3183 OH2 TIP3 170 70.261 −4.143 25.064 1.00 44.75 ATOM 3186 OH2 TIP3 171 77.519 5.882 22.891 1.00 42.67 ATOM 3189 OH2 TIP3 172 −0.921 −8.166 4.521 1.00 45.91 ATOM 3192 OH2 TIP3 173 34.213 15.329 1.478 1.00 40.10 ATOM 3195 OH2 TIP3 174 −9.647 7.731 7.383 1.00 35.63 ATOM 3198 OH2 TIP3 175 11.619 5.799 7.440 1.00 36.36 ATOM 3201 OH2 TIP3 176 −8.709 13.964 13.507 1.00 51.97 ATOM 3204 OH2 TIP3 177 31.770 3.376 18.354 1.00 46.26 ATOM 3207 OH2 TIP3 178 −8.494 9.789 24.269 1.00 50.98 ATOM 3210 OH2 TIP3 179 −1.234 −6.253 15.622 1.00 38.47 ATOM 3213 OH2 TIP3 180 80.252 0.887 15.691 1.00 39.48 ATOM 3216 OH2 TIP3 181 67.248 20.272 −1.555 1.00 48.22 ATOM 3219 OH2 TIP3 182 −0.566 4.367 1.362 1.00 39.84 ATOM 3222 OH2 TIP3 183 0.120 6.523 2.615 1.00 33.11 ATOM 3225 OH2 TIP3 184 −1.496 8.789 1.237 1.00 41.03 ATOM 3228 OH2 TIP3 185 −5.143 9.130 2.236 1.00 40.47 ATOM 3231 OH2 TIP3 186 −7.275 10.106 3.833 1.00 40.55 ATOM 3234 OH2 TIP3 187 2.717 7.275 0.769 1.00 44.67 ATOM 3237 OH2 TIP3 188 5.176 10.645 8.459 1.00 34.48 ATOM 3240 OH2 TIP3 189 63.822 12.690 22.883 1.00 41.88 ATOM 3243 OH2 TIP3 190 79.109 1.028 18.201 1.00 46.40 ATOM 3246 OH2 TIP3 191 59.332 −11.681 7.236 1.00 63.45 ATOM 3249 OH2 TIP3 192 13.Y67 −1.218 −4.268 1.00 34.79 ATOM 3252 OH2 TIP3 193 59.444 2.867 33.368 1.00 41.00 ATOM 3255 OH2 TIP3 194 32.024 13.487 19.852 1.00 53.61 ATOM 3258 OH2 TIP3 195 72.101 16.218 22.802 1.00 44.03 ATOM 3261 OH2 TIP3 196 0.987 −8.546 14.474 1.00 41.38 ATOM 3264 OH2 TIP3 197 −0.491 5.461 30.372 1.00 38.51 ATOM 3267 OH2 TIP3 198 61.179 6.795 11.905 1.00 41.77 ATOM 3270 OH2 TIP3 199 1.365 −4.128 27.656 1.00 50.98 ATOM 3273 OH2 TIP3 200 81.440 15.558 17.262 1.00 44.47 ATOM 3276 OH2 TIP3 201 −17.491 4.116 23.873 1.00 50.58 ATOM 3279 OH2 TIP3 202 27.546 10.513 14.499 1.00 39.06 ATOM 3282 OH2 TIP3 203 34.992 4.513 27.719 1.00 49.89 ATOM 3285 OH2 TIP3 204 −3.486 −4.591 9.171 1.00 49.53 ATOM 3288 OH2 TIP3 205 42.799 7.848 22.320 1.00 43.50 ATOM 3291 OH2 TIP3 206 52.728 11.884 21.811 1.00 39.98 ATOM 3294 OH2 TIP3 207 26.706 14.069 19.833 1.00 46.68 ATOM 3297 OH2 TIP3 208 −7.154 8.907 6.444 1.00 42.83 ATOM 3300 OH2 TIP3 209 86.648 5.606 16.034 1.00 51.15 ATOM 3303 OH2 TIP3 210 54.879 15.840 20.379 1.00 50.23 ATOM 3306 OH2 TIP3 211 51.417 19.473 22.691 1.00 48.35 ATOM 3309 OH2 TIP3 212 20.102 6.924 7.085 1.00 38.15 ATOM 3312 OH2 TIP3 213 28.991 1.941 −3.570 1.00 47.39 ATOM 3315 OH2 TIP3 214 26.505 2.386 −4.633 1.00 46.48 ATOM 3318 OH2 TIP3 215 36.482 2.810 18.521 1.00 46.26 ATOM 3321 OH2 TIP3 216 16.941 −20.504 14.128 1.00 49.74 ATOM 3324 OH2 TIP3 217 28.572 −14.448 6.157 1.00 49.13 ATOM 3327 OH2 TIP3 218 31.380 1.471 −1.998 1.00 43.02 ATOM 3330 OH2 TIP3 219 10.065 −16.338 15.455 1.00 42.75 ATOM 3333 OH2 TIP3 220 7.350 −11.974 5.652 1.00 55.35 ATOM 3336 OH2 TIP3 221 −12.328 14.547 10.986 1.00 51.29 ATOM 3339 OH2 TIP3 222 11.186 9.609 −1.388 1.00 37.68 ATOM 3342 OH2 TIP3 223 11.389 12.276 −1.400 1.00 46.93 ATOM 3345 OH2 TIP3 224 34.202 13.069 −1.161 1.00 41.79 ATOM 3348 OH2 TIP3 225 31.303 17.822 7.853 1.00 48.21 ATOM 3351 OH2 TIP3 226 36.875 11.804 −2.106 1.00 59.03 ATOM 3354 OH2 TIP3 227 35.134 3.048 11.020 1.00 50.41 ATOM 3357 OH2 TIP3 228 63.950 13.409 26.627 1.00 43.40 ATOM 3360 OH2 TIP3 229 36.367 6.116 15.221 1.00 57.79 ATOM 3363 OH2 TIP3 230 90.606 4.355 6.342 1.00 47.53 ATOM 3366 OH2 TIP3 231 50.038 −11.673 10.767 1.00 56.90 ATOM 3369 OH2 TIP3 232 60.196 −10.144 16.590 1.00 51.61 ATOM 3372 OH2 TIP3 233 18.021 −21.179 7.008 1.00 49.93 ATOM 3375 OH2 TIP3 234 66.236 −1.218 30.583 1.00 39.55 ATOM 3378 OH2 TIP3 235 74.959 18.928 20.659 1.00 38.04 ATOM 3381 OH2 TIP3 236 −2.816 10.082 3.187 1.00 49.31 ATOM 3384 OH2 TIP3 237 5.894 −3.410 25.289 1.00 35.55 ATOM 3387 OH2 TIP3 238 35.784 6.047 12.543 1.00 41.96 ATOM 3390 OH2 TIP3 239 −5.400 16.537 14.180 1.00 43.13 ATOM 3393 OH2 TIP3 240 46.589 −11.622 26.970 1.00 43.71 ATOM 3396 OH2 TIP3 241 6.199 6.592 13.797 1.00 46.51 ATOM 3399 OH2 TIP3 242 −3.777 −5.158 20.907 1.00 42.08 ATOM 3402 OH2 TIP3 243 1.969 −3.711 −0.282 1.00 37.38 ATOM 3405 OH2 TIP3 244 86.200 11.629 22.877 1.00 56.51 ATOM 3408 OH2 TIP3 245 10.557 7.565 5.514 1.00 47.58 ATOM 3411 OH2 TIP3 246 4.802 8.149 2.136 1.00 50.70 ATOM 3414 OH2 TIP3 247 64.590 −8.128 20.596 1.00 43.65 ATOM 3417 OH2 TIP3 248 11.346 −17.840 13.283 1.00 47.64 ATOM 3420 OH2 TIP3 249 42.116 −6.808 14.953 1.00 53.79 ATOM 3423 OH2 TIP3 250 2.745 −4.054 22.128 1.00 60.88 ATOM 3426 OH2 TIP3 251 71.999 1.177 −2.124 1.00 47.90 ATOM 3429 OH2 TIP3 252 50.328 −3.210 33.068 1.00 57.01 ATOM 3435 OH2 TIP3 253 57.838 9.337 11.631 1.00 52.55 ATOM 3438 OH2 TIP3 254 43.373 20.489 30.490 1.00 51.97 ATOM 3441 OH2 TIP3 255 67.045 16.529 15.793 1.00 49.02 ATOM 3444 OH2 TIP3 256 87.509 21.566 5.114 1.00 54.21 ATOM 3447 OH2 TIP3 257 21.060 10.052 −9.215 1.00 60.32 ATOM 3450 OH2 TIP3 258 11.827 2.450 27.951 1.00 54.26 ATOM 3453 OH2 TIP3 259 64.788 −0.418 3.563 1.00 50.94 ATOM 3456 OH2 TIP3 260 71.859 28.473 7.950 1.00 62.81 ATOM 3459 OH2 TIP3 261 25.605 −8.106 27.287 1.00 52.81 ATOM 3462 OH2 TIP3 262 −18.804 10.886 12.628 1.00 55.25 ATOM 3465 OH2 TIP3 263 30.652 11.349 16.201 1.00 50.40 ATOM 3468 OH2 TIP3 264 22.350 −16.098 −2.742 1.00 53.27 ATOM 3471 OH2 TIP3 265 29.720 9.106 18.465 1.00 57.23

[0130] TABLE 4 Atomic Structure Coordinates of Unphosphorylated FLGK:AMP-PCP Co-Complex Atom A.A. A.A. Atom No. Type Type No. X Y Z OCC B ATOM 1 N GLU 1464 −13.425 16.769 8.973 1.00 61.21 ATOM 3 CA GLU 1464 −12.536 16.852 7.821 1.00 59.70 ATOM 4 CB GLU 1464 −11.383 17.829 8.085 1.00 60.05 ATOM 5 C GLU 1464 −11.998 15.478 7.427 1.00 57.11 ATOM 6 O GLU 1464 −12.134 15.076 6.274 1.00 59.75 ATOM 7 N LEU 1465 −11.406 14.749 8.368 1.00 52.21 ATOM 9 CA LEU 1465 −10.871 13.424 8.062 1.00 46.72 ATOM 10 CB LEU 1465 −10.102 12.844 9.249 1.00 44.98 ATOM 11 CG LEU 1465 −8.608 13.123 9.384 1.00 46.11 ATOM 12 CD1 LEU 1465 −8.338 14.592 9.663 1.00 51.13 ATOM 13 CD2 LEU 1465 −8.064 12.286 10.512 1.00 4.99 ATOM 14 C LEU 1465 −12.000 12.475 7.700 1.00 44.16 ATOM 15 O LEU 1465 −13.101 12.577 8.239 1.00 44.04 ATOM 16 N PRO 1466 −11.760 11.580 6.732 1.00 42.53 ATOM 17 CD PRO 1466 −10.535 11.534 5.913 1.00 41.30 ATOM 18 CA PRO 1466 −12.740 10.591 6.269 1.00 41.16 ATOM 19 CB PRO 1466 −12.134 10.111 4.959 1.00 41.48 ATOM 20 CG PRO 1466 −10.658 10.213 5.220 1.00 41.30 ATOM 21 C PRO 1466 −12.906 9.441 7.261 1.00 41.31 ATOM 22 O PRO 1466 −11.929 8.936 7.816 1.00 41.05 ATOM 23 N GLU 1467 −14.145 9.044 7.500 1.00 41.02 ATOM 25 CA GLU 1467 −14.428 7.960 8.427 1.00 42.42 ATOM 26 CB GLU 1467 −15.931 7.904 8.712 1.00 47.98 ATOM 27 CG GLU 1467 −16.565 9.238 9.105 1.00 52.79 ATOM 28 CD GLU 1467 −17.998 9.093 9.606 1.00 54.21 ATOM 29 OE1 GLU 1467 −18.474 7.949 9.741 1.00 58.90 ATOM 30 OE2 GLU 1467 −18.650 10.120 9.879 1.00 55.90 ATOM 31 C GLU 1467 −13.972 6.628 7.837 1.00 40.93 ATOM 32 O GLU 1467 −14.061 6.426 6.620 1.00 44.32 ATOM 33 N ASP 1468 −13.473 5.731 8.689 1.00 35.10 ATOM 35 CA ASP 1468 −13.024 4.404 8.256 1.00 31.82 ATOM 36 CB ASP 1468 −11.507 4.358 7.992 1.00 30.65 ATOM 37 CG ASP 1468 −11.025 3.002 7.440 1.00 29.93 ATOM 38 OD1 ASP 1468 −11.689 1.958 7.603 1.00 29.63 ATOM 39 OD2 ASP 1468 −9.945 2.974 6.835 1.00 33.63 ATOM 40 C ASP 1468 −13.394 3.441 9.369 1.00 31.81 ATOM 41 O ASP 1468 −12.618 3.209 10.302 1.00 31.91 ATOM 42 N PRO 1469 −14.569 2.819 9.247 1.00 29.68 ATOM 43 CD PRO 1469 −15.482 2.963 8.097 1.00 28.33 ATOM 44 CA PRO 1469 −15.100 1.863 10.220 1.00 31.80 ATOM 45 CB PRO 1469 −16.352 1.331 9.510 1.00 32.51 ATOM 46 CG PRO 1469 −16.783 2.496 8.656 1.00 27.41 ATOM 47 C PRO 1469 −14.146 0.731 10.590 1.00 30.44 ATOM 48 O PRO 1469 −14.272 0.135 11.654 1.00 30.02 ATOM 49 N ARG 1470 −13.198 0.442 9.704 1.00 31.06 ATOM 51 CA ARG 1470 −12.240 −0.636 9.917 1.00 31.86 ATOM 52 CB ARG 1470 −11.386 −0.860 8.660 1.00 31.36 ATOM 53 CG ARG 1470 −12.107 −1.437 7.448 1.00 33.08 ATOM 54 CD ARG 1470 −11.148 −1.588 6.248 1.00 31.08 ATOM 55 NE ARG 1470 −10.540 −0.310 5.891 1.00 34.36 ATOM 57 CZ ARG 1470 −9.656 −0.135 4.919 1.00 33.32 ATOM 58 NH1 ARG 1470 −9.260 −1.164 4.185 1.00 35.90 ATOM 61 NH2 ARG 1470 −9.155 1.074 4.687 1.00 32.79 ATOM 64 C ARG 1470 −11.290 −0.436 11.095 1.00 32.68 ATOM 65 O ARG 1470 −10.820 −1.410 11.683 1.00 33.43 ATOM 66 N TRP 1471 −11.031 0.814 11.456 1.00 31.84 ATOM 68 CA TRP 1471 −10.063 1.090 12.505 1.00 31.17 ATOM 69 CB TRP 1471 −8.816 1.677 11.850 1.00 30.15 ATOM 70 CO TRP 1471 −8.173 0.725 10.941 1.00 29.54 ATOM 71 CD2 TRP 1471 −7.288 −0.329 11.315 1.00 31.07 ATOM 72 CE2 TRP 1471 −6.913 −0.992 10.132 1.00 34.41 ATOM 73 CE3 TRP 1471 −6.762 −0.768 12.536 1.00 29.46 ATOM 74 CD1 TRP 1471 −8.309 0.660 9.587 1.00 30.20 ATOM 75 NEl TRP 1471 −7.557 −0.371 9.089 1.00 33.09 ATOM 77 CZ2 TRP 1471 −6.042 −2.085 10.135 1.00 31.68 ATOM 78 CZ3 TRP 1471 −5.897 −1.853 12.540 1.00 29.65 ATOM 79 CH2 TRP 1471 −5.541 −2.494 11.347 1.00 30.18 ATOM 80 C TRP 1471 −10.477 2.019 13.620 1.00 29.94. ATOM 81 O TRP 1471 −9.782 2.108 14.631 1.00 30.00 ATOM 82 N GLU 1472 −11.573 2.737 13.416 1.00 29.06 ATOM 84 CA GLU 1472 −12.051 3.706 14.380 1.00 28.62 ATOM 85 CB GLU 1472 −13.312 4.386 13.849 1.00 29.16 ATOM 86 CO GLU 1472 −13.641 5.733 14.529 1.00 30.74 ATOM 87 CD GLU 1472 −12.676 6.848 14.156 1.00 30.05 ATOM 88 OE1 GLU 1472 −12.090 6.799 13.057 1.00 31.32 ATOM 89 OE2 GLU 1472 −12.511 7.784 14.961 1.00 30.26 ATOM 90 C GLU 1472 −12.327 3.159 15.767 1.00 28.70 ATOM 91 O GLU 1472 −12.969 2.125 15.916 1.00 31.01 ATOM 92 N LEU 1473 −11.810 3.842 16.781 1.00 27.38 ATOM 94 CA LEU 1473 −12.054 3.451 18.161 1.00 29.61 ATOM 95 CB LEU 1473 −10.763 3.073 18.899 1.00 28.56 ATOM 96 CG LEU 1473 −10.923 2.756 20.403 1.00 30.06 ATOM 97 CD1 LEU 1473 −11.485 1.354 20.639 1.00 28.42 ATOM 98 CD2 LEU 1473 −9.595 2.876 21.115 1.00 28.15 ATOM 99 C LEU 1473 −12.617 4.714 18.764 1.00 31.81 ATOM 100 O LEU 1473 −12.179 5.814 18.407 1.00 33.00 ATOM 101 N PRO 1474 −13.670 4.591 19.596 1.00 31.45 ATOM 102 CD PRO 1474 −14.488 3.400 19.859 1.00 31.72 ATOM 103 CA PRO 1474 −14.261 5.774 20.226 1.00 31.23 ATOM 104 CE PRO 1474 −15.400 5.176 21.048 1.00 29.01 ATOM 105 CG PRO 1474 −15.815 4.005 20.247 1.00 29.09 ATOM 106 C PRO 1474 −13.217 6.444 21.120 1.00 33.36 ATOM 107 O PRO 1474 −12.447 5.765 21.808 1.00 36.40 ATOM 108 N ARG 1475 −13.188 7.770 21.112 1.00 33.67 ATOM 110 CA ARG 1475 −12.228 8.498 21.924 1.00 33.96 ATOM 111 CE ARG 1475 −12.433 9.991 21.735 1.00 35.31 ATOM 112 CO ARG 1475 −12.134 10.405 20.333 1.00 40.10 ATOM 113 CD ARG 1475 −12.060 11.906 20.145 1.00 42.98 ATOM 114 NE ARG 1475 −11.785 12.194 18.737 1.00 42.91 ATOM 116 CZ ARG 1475 −10.578 12.443 18.253 1.00 41.30 ATOM 117 NH1 ARG 1475 −9.529 12.467 19.064 1.00 41.88 ATOM 120 NH2 ARG 1475 −10.413 12.567 16.943 1.00 40.98 ATOM 123 C ARG 1475 −12.278 8.142 23.404 1.00 35.88 ATOM 124 O ARG 1475 −11.240 8.046 24.061 1.00 37.10 ATOM 125 N ASP 1476 −13.479 7.920 23.928 1.00 36.47 ATOM 127 CA ASP 1476 −13.632 7.581 25.335 1.00 37.24 ATOM 128 CE ASP 1476 −15.112 7.629 25.741 1.00 39.66 ATOM 129 CO ASP 1476 −15.930 6.480 25.163 1.00 42.38 ATOM 130 OD1 ASP 1476 −15.438 5.706 24.322 1.00 47.52 ATOM 131 OD2 ASP 1476 −17.098 6.349 25.568 1.00 48.06 ATOM 132 C ASP 1476 −13.023 6.232 25.724 1.00 36.93 ATOM 133 O ASP 1476 −13.034 5.856 26.898 1.00 40.09 ATOM 134 N ARG 1477 −12.564 5.475 24.732 1.00 34.34 ATOM 136 CA ARG 1477 −11.961 4.171 24.993 1.00 32.47 ATOM 137 CB ARG 1477 −12.269 3.212 23.852 1.00 31.59 ATOM 138 CG ARG 1477 −13.716 2.939 23.640 1.00 29.66 ATOM 139 CD ARG 1477 −14.314 2.342 24.875 1.00 30.65 ATOM 140 NE ARG 1477 −14.498 3.342 25.918 1.00 31.37 ATOM 142 CZ ARG 1477 −14.822 3.055 27.174 1.00 32.81 ATOM 143 NH1 ARG 1477 −15.002 1.794 27.549 1.00 33.92 ATOM 146 NH2 ARG 1477 −14.950 4.025 28.062 1.00 31.74 ATOM 149 C ARG 1477 −10.452 4.266 25.153 1.00 33.13 ATOM 150 O ARG 1477 −9.777 3.281 25.445 1.00 33.55 ATOM 151 N LEU 1478 −9.923 5.466 24.984 1.00 34.43 ATOM 153 CA LEU 1478 −8.493 5.663 25.076 1.00 35.68 ATOM 154 CB LEU 1478 −8.008 6.350 23.790 1.00 34.98 ATOM 155 CG LEU 1478 −6.581 6.137 23.284 1.00 31.11 ATOM 156 CD1 LEU 1478 −6.280 4.650 23.161 1.00 26.62 ATOM 157 CD2 LEU 1478 −6.428 6.839 21.940 1.00 28.80 ATOM 158 C LEU 1478 −8.158 6.505 26.295 1.00 36.21 ATOM 159 O LEU 1478 −8.501 7.688 26.361 1.00 39.67 ATOM 160 N VAL 1479 −7.558 5.878 27.293 1.00 35.42 ATOM 162 CA VAL 1479 −7.156 6.599 28.491 1.00 35.80 ATOM 163 CB VAL 1479 −7.269 5.707 29.742 1.00 36.29 ATOM 164 CG1 VAL 1479 −7.017 6.527 30.983 1.00 37.23 ATOM 165 CG2 VAL 1479 −8.650 5.059 29.812 1.00 34.41 ATOM 166 C VAL 1479 −5.704 7.046 28.244 1.00 35.68 ATOM 167 O VAL 1479 −4.764 6.246 28.319 1.00 33.45 ATOM 168 N LEU 1480 −5.538 8.315 27.885 1.00 38.15 ATOM 170 CA LEU 1480 −4.213 8.860 27.584 1.00 42.61 ATOM 171 CB LEU 1480 −4.332 10.205 26.857 1.00 39.14 ATOM 172 CG LEU 1480 −4.969 10.179 25.460 1.00 38.44 ATOM 173 CD1 LEU 1480 −4.901 11.579 24.879 1.00 39.39 ATOM 174 CD2 LEU 1480 −4.263 9.194 24.533 1.00 36.86 ATOM 175 C LEU 1480 −3.274 8.970 28.783 1.00 46.37 ATOM 176 O LEU 1480 −3.659 9.445 29.850 1.00 48.86 ATOM 177 N GLY 1481 −2.033 8.537 28.594 1.00 47.13 ATOM 179 CA GLY 1481 −1.081 8.573 29.678 1.00 48.19 ATOM 180 C GLY 1481 0.163 9.388 29.425 1.00 50.27 ATOM 181 O GLY 1481 0.152 10.367 28.675 1.00 51.19 ATOM 182 N LYS 1482 1.240 8.965 30.078 1.00 50.93 ATOM 184 CA LYS 1482 2.543 9.606 30.007 1.00 50.94 ATOM 185 CB LYS 1482 3.509 8.866 30.933 1.00 50.41 ATOM 186 CG LYS 1482 4.971 9.026 30.567 1.00 51.87 ATOM 187 CD LYS 1482 5.810 7.874 31.087 1.00 53.49 ATOM 188 CE LYS 1482 5.390 6.542 30.478 1.00 50.77 ATOM 189 NZ LYS 1482 6.251 5.433 30.986 1.00 49.92 ATOM 193 C LYS 1482 3.145 9.676 28.609 1.00 52.31 ATOM 194 O LYS 1482 3.115 8.700 27.851 1.00 52.30 ATOM 195 N PRO 1483 3.706 10.838 28.250 1.00 53.47 ATOM 196 CD PRO 1483 3.667 12.105 28.997 1.00 54.19 ATOM 197 CA PRO 1483 4.326 11.021 26.937 1.00 54.10 ATOM 198 CB PRO 1483 4.772 12.480 26.976 1.00 54.25 ATOM 199 CG PRO 1483 3.772 13.118 27.895 1.00 55.30 ATOM 200 C PRO 1483 5.535 10.096 26.827 1.00 54.72 ATOM 201 O PRO 1483 6.343 10.017 27.751 1.00 53.48 ATOM 202 N LEU 1484 5.619 9.351 25.731 1.00 57.05 ATOM 204 CA LEU 1484 6.739 8.447 25.503 1.00 59.26 ATOM 205 CB LEU 1484 6.307 7.241 24.669 1.00 59.35 ATOM 206 CG LEU 1484 5.391 6.216 25.343 1.00 60.87 ATOM 207 CD1 LEU 1484 4.975 5.161 24.329 1.00 57.14 ATOM 208 CD2 LEU 1484 6.081 5.571 26.551 1.00 59.79 ATOM 209 C LEU 1484 7.847 9.194 24.778 1.00 61.30 ATOM 210 O LEU 1484 8.980 8.720 24.701 1.00 62.17 ATOM 211 N GLY 1485 7.494 10.351 24.220 1.00 63.75 ATOM 213 CA GLY 1485 8.456 11.173 23.507 1.00 66.33 ATOM 214 C GLY 1485 8.081 11.412 22.054 1.00 67.79 ATOM 215 O GLY 1485 6.918 11.653 21.727 1.00 69.61 ATOM 216 N GLN 1491 4.615 13.762 18.385 1.00 58.26 ATOM 218 CA GLN 1491 4.353 13.353 19.762 1.00 57.98 ATOM 219 CB GLN 1491 3.476 14.379 20.468 1.00 61.80 ATOM 220 CG GLN 1491 3.134 14.034 21.920 1.00 70.31 ATOM 221 CD GLN 1491 2.019 14.911 22.482 1.00 75.91 ATOM 222 OE1 GLN 1491 1.355 15.636 21.748 1.00 77.85 ATOM 223 NE2 GLN 1491 1.820 14.832 23.788 1.00 78.30 ATOM 226 C GLN 1491 3.709 11.965 19.881 1.00 54.67 ATOM 227 O GLN 1491 2.701 11.669 19.222 1.00 54.91 ATOM 228 N VAL 1492 4.305 11.125 20.729 1.00 50.04 ATOM 230 CA VAL 1492 3.825 9.763 20.988 1.00 44.93 ATOM 231 CE VAL 1492 4.861 8.705 20.583 1.00 42.65 ATOM 232 CG1 VAL 1492 4.378 7.325 20.958 1.00 39.71 ATOM 233 CG2 VAL 1492 5.119 8.766 19.099 1.00 40.98 ATOM 234 C VAL 1492 3.584 9.661 22.490 1.00 43.43 ATOM 235 O VAL 1492 4.451 10.029 23.289 1.00 43.43 ATOM 236 N VAL 1493 2.400 9.212 22.888 1.00 41.13 ATOM 238 CA VAL 1493 2.107 9.080 24.304 1.00 38.77 ATOM 239 CB VAL 1493 1.052 10.133 24.782 1.00 36.35 ATOM 240 CG1 VAL 1493 1.410 11.508 24.287 1.00 36.06 ATOM 241 CG2 VAL 1493 −0.329 9.755 24.339 1.00 37.64 ATOM 242 C VAL 1493 1.589 7.693 24.619 1.00 37.77 ATOM 243 O VAL 1493 0.948 7.058 23.783 1.00 38.88 ATOM 244 N LEU 1494 1.949 7.187 25.790 1.00 36.24 ATOM 246 CA LEU 1494 1.468 5.880 26.205 1.00 35.92 ATOM 247 CB LEU 1494 2.252 5.383 27.429 1.00 35.41 ATOM 248 CG LEU 1494 1.886 4.009 28.004 1.00 36.21 ATOM 249 CD1 LEU 1494 1.927 2.931 26.924 1.00 33.60 ATOM 250 CD2 LEU 1494 2.835 3.670 29.145 1.00 36.03 ATOM 251 C LEU 1494 −0.010 6.095 26.564 1.00 35.27 ATOM 252 O LEU 1494 −0.425 7.215 26.887 1.00 34.35 ATOM 253 N ALA 1495 −0.807 5.043 26.468 1.00 34.93 ATOM 255 CA ALA 1495 −2.220 5.145 26.768 1.00 34.44 ATOM 256 CB ALA 1495 −2.955 5.794 25.616 1.00 35.29 ATOM 257 C ALA 1495 −2.781 3.770 27.018 1.00 34.59 ATOM 258 O ALA 1495 −2.128 2.766 26.748 1.00 35.52 ATOM 259 N GLU 1496 −3.996 3.723 27.536 1.00 36.64 ATOM 261 CA GLU 1496 −4.652 2.462 27.806 1.00 37.57 ATOM 262 CE GLU 1496 −5.000 2.354 29.287 1.00 38.97 ATOM 263 CG GLU 1496 −3.769 2.304 30.185 1.00 41.79 ATOM 264 CD GLU 1496 −4.110 2.475 31.645 1.00 43.65 ATOM 265 OE1 GLU 1496 −4.408 3.617 32.036 1.00 42.97 ATOM 266 OE2 GLU 1496 −4.086 1.475 32.398 1.00 46.65 ATOM 267 C GLU 1496 −5.896 2.404 26.943 1.00 38.50 ATOM 268 O GLU 1496 −6.660 3.371 26.867 1.00 40.28 ATOM 269 N ALA 1497 −6.051 1.301 26.223 1.00 37.34 ATOM 271 CA ALA 1497 −7.194 1.131 25.352 1.00 37.42 ATOM 272 CE ALA 1497 −6.743 0.625 23.985 1.00 35.92 ATOM 273 C ALA 1497 −8.146 0.148 26.000 1.00 36.77 ATOM 274 O ALA 1497 −7.759 −0.977 26.323 1.00 35.74 ATOM 275 N ILE 1498 −9.354 0.616 26.291 1.00 37.03 ATOM 277 CA ILE 1498 −10.378 −0.224 26.896 1.00 36.80 ATOM 278 CE ILE 1498 −11.372 0.612 27.728 1.00 34.53 ATOM 279 CG2 ILE 1498 −12.373 −0.290 28.425 1.00 34.59 ATOM 280 CG1 ILE 1498 −10.640 1.438 28.778 1.00 31.97 ATOM 281 CD1 ILE 1498 −11.552 2.344 29.541 1.00 31.12 ATOM 282 C ILE 1498 −11.126 −0.807 25.709 1.00 38.72 ATOM 283 O ILE 1498 −11.647 −0.066 24.879 1.00 37.74 ATOM 284 N GLY 1499 −11.137 −2.126 25.590 1.00 40.98 ATOM 286 CA GLY 1499 −11.839 −2.728 24.482 1.00 44.64 ATOM 287 C GLY 1499 −10.931 −3.115 23.332 1.00 48.45 ATOM 288 O GLY 1499 −10.260 −4.147 23.401 1.00 51.92 ATOM 289 N LEU 1500 −10.877 −2.269 22.303 1.00 47.87 ATOM 291 CA LEU 1500 −10.076 −2.530 21.102 1.00 46.80 ATOM 292 CB LEU 1500 −8.594 −2.770 21.434 1.00 45.37 ATOM 293 CG LEU 1500 −7.543 −1.661 21.293 1.00 44.84 ATOM 294 CD1 LEU 1500 −6.174 −2.290 21.450 1.00 43.33 ATOM 295 CD2 LEU 1500 −7.623 −0.959 19.948 1.00 40.43 ATOM 296 C LEU 1500 −10.631 −3.737 20.349 1.00 45.63 ATOM 297 O LEU 1500 −10.797 −4.823 20.915 1.00 44.42 ATOM 298 N PRO 1505 −13.569 −5.910 25.549 1.00 52.13 ATOM 299 CD PRO 1505 −14.316 −7.170 25.398 1.00 54.09 ATOM 300 CA PRO 1505 −14.451 −4.828 25.999 1.00 50.46 ATOM 301 CB PRO 1505 −15.841 −5.455 25.891 1.00 49.86 ATOM 302 CG PRO 1505 −15.586 −6.898 26.193 1.00 52.17 ATOM 303 C PRO 1505 −14.136 −4.370 27.422 1.00 47.75 ATOM 304 O PRO 1505 −14.148 −3.180 27.710 1.00 47.93 ATOM 305 N ASN 1506 −13.778 −5.313 28.285 1.00 46.20 ATOM 307 CA ASN 1506 −13.458 −4.986 29.666 1.00 49.52 ATOM 308 CB ASN 1506 −14.310 −5.829 30.612 1.00 52.42 ATOM 309 CG ASN 1506 −15.788 −5.489 30.526 1.00 54.50 ATOM 310 OD1 ASN 1506 −16.179 −4.331 30.680 1.00 57.16 ATOM 311 ND2 ASN 1506 −16.610 −6.489 30.244 1.00 56.82 ATOM 314 C ASN 1506 −11.973 −5.124 30.003 1.00 50.65 ATOM 315 O ASN 1506 −11.583 −5.174 31.178 1.00 50.65 ATOM 316 N ARG 1507 −11.142 −5.145 28.968 1.00 50.90 ATOM 318 CA ARG 1507 −9.700 −5.276 29.127 1.00 49.77 ATOM 319 CB ARG 1507 −9.192 −6.483 28.339 1.00 55.81 ATOM 320 CG ARG 1507 −9.450 −7.833 28.988 1.00 61.63 ATOM 321 CD ARG 1507 −8.408 −8.149 30.041 1.00 66.01 ATOM 322 NE ARG 1507 −8.600 −9.490 30.583 1.00 72.55 ATOM 324 CZ ARG 1507 −8.024 −9.944 31.694 1.00 77.32 ATOM 325 NH1 ARG 1507 −7.198 −9.169 32.392 1.00 78.41 ATOM 328 NH2 ARG 1507 −8.335 −11.151 32.147 1.00 79.30 ATOM 331 C ARG 1507 −9.015 −4.036 28.595 1.00 45.60 ATOM 332 O ARG 1507 −9.452 −3.464 27.590 1.00 42.08 ATOM 333 N VAL 1508 −7.977 −3.597 29.297 1.00 42.86 ATOM 335 CA VAL 1508 −7.216 −2.443 28.858 1.00 40.75 ATOM 336 CB VAL 1508 −6.903 −1.428 30.010 1.00 38.75 ATOM 337 CG1 VAL 1508 −8.184 −1.015 30.702 1.00 43.29 ATOM 338 CG2 VAL 1508 −5.919 −2.005 31.012 1.00 37.56 ATOM 339 C VAL 1508 −5.929 −2.970 28.248 1.00 39.14 ATOM 340 O VAL 1508 −5.369 −3.972 28.708 1.00 39.16 ATOM 341 N TER 1509 −5.517 −2.345 27.157 1.00 37.26 ATOM 343 CA TER 1509 −4.298 −2.737 26.486 1.00 36.52 ATOM 344 CB TER 1509 −4.571 −3.187 25.019 1.00 37.83 ATOM 345 OG1 TER 1509 −5.423 −4.340 25.011 1.00 43.88 ATOM 347 CG2 TER 1509 −3.267 −3.540 24.310 1.00 34.51 ATOM 348 C TER 1509 −3.434 −1.495 26.473 1.00 35.82 ATOM 349 O TER 1509 −3.927 −0.408 26.174 1.00 34.37 ATOM 350 N LYS 1510 −2.175 −1.628 26.880 1.00 35.96 ATOM 352 CA LYS 1510 −1.291 −0.479 26.843 1.00 36.13 ATOM 353 CB LYS 1510 −0.032 −0.695 27.680 1.00 37.77 ATOM 354 CG LYS 1510 −0.277 −0.854 29.162 1.00 44.58 ATOM 355 CD LYS 1510 1.023 −0.658 29.948 1.00 51.33 ATOM 356 CE LYS 1510 0.947 −1.286 31.342 1.00 58.15 ATOM 357 NZ LYS 1510 −0.149 −0.728 32.187 1.00 64.94 ATOM 361 C LYS 1510 −0.929 −0.355 25.373 1.00 34.59 ATOM 362 O LYS 1510 −0.574 −1.345 24.734 1.00 31.43 ATOM 363 N VAL 1511 −1.092 0.846 24.835 1.00 32.95 ATOM 365 CA VAL 1511 −0.810 1.121 23.441 1.00 32.29 ATOM 366 CB VAL 1511 −2.129 1.213 22.621 1.00 32.95 ATOM 367 CG1 VAL 1511 −2.879 −0.109 22.686 1.00 34.79 ATOM 368 CG2 VAL 1511 −3.026 2.354 23.148 1.00 32.84 ATOM 369 C VAL 1511 −0.058 2.446 23.353 1.00 32.65 ATOM 370 O VAL 1511 0.021 3.185 24.344 1.00 31.62 ATOM 371 N ALA 1512 0.521 2.721 22.186 1.00 30.24 ATOM 373 CA ALA 1512 1.244 3.969 21.954 1.00 28.18 ATOM 374 CB ALA 1512 2.599 3.700 21.316 1.00 25.62 ATOM 375 C ALA 1512 0.373 4.783 21.015 1.00 27.54 ATOM 376 O ALA 1512 −0.151 4.264 20.040 1.00 27.17 ATOM 377 N VAL 1513 0.204 6.054 21.322 1.00 30.52 ATOM 379 CA VAL 1513 −0.630 6.914 20.503 1.00 34.08 ATOM 380 CB VAL 513 −1.731 7.591 21.347 1.00 34.61 ATOM 381 CG1 VAL 1513 −2.607 8.444 20.474 1.00 36.75 ATOM 382 CG2 VAL 1513 −2.567 6.549 22.087 1.00 33.45 ATOM 383 C VAL 1513 0.203 8.008 19.837 1.00 36.38 ATOM 384 O VAL 1513 0.924 8.750 20.510 1.00 35.32 ATOM 385 N LYS 1514 0.105 8.093 18.513 1.00 38.19 ATOM 387 CA LYS 1514 0.818 9.104 17.746 1.00 40.12 ATOM 388 CB LYS 1514 1.339 8.513 16.439 1.00 40.93 ATOM 389 CG LYS 1514 2.452 7.488 16.632 1.00 42.52 ATOM 390 CD LYS 1514 2.861 6.803 15.338 1.00 46.25 ATOM 391 CE LYS 1514 3.268 7.796 14.261 1.00 49.76 ATOM 392 NZ LYS 1514 4.304 8.771 14.705 1.00 52.14 ATOM 396 C LYS 1514 −0.166 10.215 17.458 1.00 40.69 ATOM 397 O LYS 1514 −1.313 9.953 17.110 1.00 41.69 ATOM 398 N MET 1515 0.277 11.454 17.613 1.00 43.28 ATOM 400 CA MET 1515 −0.569 12.610 17.379 1.00 46.21 ATOM 401 CB MET 1515 −1.363 12.936 18.644 1.00 46.96 ATOM 402 CG MET 1515 −0.488 13.293 19.837 1.00 47.61 ATOM 403 SD MET 1515 −1.413 13.464 21.358 1.00 49.77 ATOM 404 CE MET 1515 −1.593 11.761 21.814 1.00 47.84 ATOM 405 C MET 1515 0.299 13.805 17.000 1.00 49.90 ATOM 406 O MET 1515 1.519 13.788 17.194 1.00 49.83 ATOM 407 N LEU 1516 −0.339 14.822 16.430 1.00 54.45 ATOM 409 CA LEU 1516 0.335 16.053 16.023 1.00 57.57 ATOM 410 CB LEU 1516 −0.483 16.762 14.944 1.00 54.10 ATOM 411 CG LEU 1516 −0.800 16.007 13.664 1.00 50.71 ATOM 412 CD1 LEU 1516 −1.830 16.800 12.901 1.00 51.20 ATOM 413 CD2 LEU 1516 0.467 15.809 12.849 1.00 50.08 ATOM 414 C LEU 1516 0.487 17.010 17.202 1.00 61.88 ATOM 415 O LEU 1516 −0.170 16.852 18.235 1.00 63.30 ATOM 416 N LYS 1517 1.335 18.018 17.021 1.00 66.83 ATOM 418 CA LYS 1517 1.568 19.036 18.037 1.00 71.46 ATOM 419 CB LYS 1517 2.985 19.593 17.911 1.00 76.28 ATOM 420 CG LYS 1517 4.084 18.626 18.349 1.00 82.19 ATOM 421 CD LYS 1517 5.450 19.085 17.846 1.00 86.93 ATOM 422 CE LYS 1517 6.579 18.228 18.411 1.00 90.46 ATOM 423 NZ LYS 1517 7.896 18.513 17.763 1.00 92.51 ATOM 427 C LYS 1517 0.549 20.156 17.837 1.00 72.44 ATOM 428 O LYS 1517 −0.142 20.198 16.819 1.00 72.12 ATOM 429 N SER 1518 0.474 21.075 18.793 1.00 73.90 ATOM 431 CA SER 1518 −0.470 22.185 18.697 1.00 74.96 ATOM 432 CB SER 1518 −0.498 22.980 20.002 1.00 74.72 ATOM 433 C SER 1518 −0.133 23.100 17.525 1.00 76.16 ATOM 434 O SER 1518 −1.029 23.667 16.897 1.00 76.56 ATOM 435 N ASP 1519 1.158 23.245 17.232 1.00 77.24 ATOM 437 CA ASP 1519 1.601 24.094 16.125 1.00 78.51 ATOM 438 CB ASP 1519 2.849 24.888 16.535 1.00 79.70 ATOM 439 C ASP 1519 1.887 23.264 14.865 1.00 78.29 ATOM 440 O ASP 1519 2.797 23.580 14.088 1.00 78.52 ATOM 441 N ALA 1520 1.121 22.192 14.682 1.00 76.90 ATOM 443 CA ALA 1520 1.285 21.313 13.529 1.00 74.09 ATOM 444 CB ALA 1520 0.737 19.930 13.840 1.00 74.20 ATOM 445 C ALA 1520 0.580 21.895 12.318 1.00 71.82 ATOM 446 O ALA 1520 −0.573 22.311 12.400 1.00 71.78 ATOM 447 N THR 1521 1.291 21.951 11.202 1.00 69.97 ATOM 449 CA THR 1521 0.734 22.480 9.970 1.00 68.86 ATOM 450 CB THR 1521 1.848 22.911 9.026 1.00 68.87 ATOM 451 OG1 THR 1521 2.621 21.762 8.651 1.00 70.03 ATOM 453 CG2 THR 1521 2.756 23.912 9.715 1.00 71.55 ATOM 454 C THR 1521 −0.081 21.389 9.292 1.00 67.89 ATOM 455 O THR 1521 0.111 20.204 9.563 1.00 69.03 ATOM 456 N GLU 1522 −0.964 21.783 8.382 1.00 66.59 ATOM 458 CA GLU 1522 −1.785 20.821 7.657 1.00 65.71 ATOM 459 CB GLU 1522 −2.737 21.532 6.692 1.00 65.61 ATOM 460 C GLU 1522 −0.886 19.823 6.909 1.00 64.32 ATOM 461 O GLU 1522 −1.324 18.729 6.549 1.00 66.29 ATOM 462 N LYS 1523 0.367 20.205 6.677 1.00 59.93 ATOM 464 CA LYS 1523 1.314 19.326 6.016 1.00 57.38 ATOM 465 CB LYS 1523 2.629 20.064 5.747 1.00 60.47 ATOM 466 CG LYS 1523 3.815 19.162 5.370 1.00 62.75 ATOM 467 CD LYS 1523 3.510 18.288 4.160 1.00 63.95 ATOM 468 CE LYS 1523 4.759 17.596 3.652 1.00 65.88 ATOM 469 NZ LYS 1523 4.429 16.721 2.494 1.00 70.37 ATOM 473 C LYS 1523 1.565 18.173 6.974 1.00 54.80 ATOM 474 O LYS 1523 1.548 17.003 6.581 1.00 54.44 ATOM 475 N ASP 1524 1.786 18.523 8.239 1.00 51.67 ATOM 477 CA ASP 1524 2.036 17.549 9.295 1.00 49.43 ATOM 478 CB ASP 1524 2.297 18.271 10.622 1.00 51.06 ATOM 479 CG ASP 1524 3.598 19.080 10.613 1.00 54.03 ATOM 480 OD1 ASP 1524 3.649 20.136 11.283 1.00 56.32 ATOM 481 OD2 ASP 1524 4.580 18.658 9.956 1.00 56.02 ATOM 482 C ASP 1524 0.847 16.596 9.413 1.00 47.73 ATOM 483 O ASP 1524 1.017 15.387 9.580 1.00 45.85 ATOM 484 N LEU 1525 −0.354 17.155 9.300 1.00 47.62 ATOM 486 CA LEU 1525 −1.585 16.380 9.354 1.00 45.95 ATOM 487 CB LEU 1525 −2.801 17.307 9.271 1.00 43.61 ATOM 488 CG LEU 1525 −4.193 16.665 9.234 1.00 44.56 ATOM 489 CD1 LEU 1525 −4.364 15.543 10.268 1.00 46.02 ATOM 490 CD2 LEU 1525 −5.215 17.740 9.468 1.00 43.80 ATOM 491 C LEU 1525 −1.605 15.372 8.210 1.00 45.67 ATOM 492 O LEU 1525 −1.921 14.204 8.416 1.00 46.78 ATOM 493 N SER 1526 −1.245 15.822 7.014 1.00 45.44 ATOM 495 CA SER 1526 −1.211 14.945 5.851 1.00 46.33 ATOM 496 CB SER 1526 −0.903 15.744 4.584 1.00 48.48 ATOM 497 OG SER 1526 −2.012 16.546 4.218 1.00 57.28 ATOM 499 C SER 1526 −0.192 13.821 5.995 1.00 43.84 ATOM 500 O SER 1526 −0.480 12.669 5.674 1.00 45.24 ATOM 501 N ASP 1527 0.994 14.144 6.489 1.00 40.88 ATOM 503 CA ASP 1527 2.024 13.128 6.646 1.00 39.70 ATOM 504 CB ASP 1527 3.376 13.767 6.960 1.00 37.62 ATOM 505 CG ASP 1527 3.934 14.555 5.786 1.00 37.01 ATOM 506 OD1 ASP 1527 3.39.9 14.434 4.657 1.00 35.78 ATOM 507 OD2 ASP 1527 4.916 15.295 5.992 1.00 40.23 ATOM 508 C ASP 1527 1.652 12.053 7.659 1.00 38.51 ATOM 509 O ASP 1527 1.951 10.872 7.461 1.00 37.68 ATOM 510 N LEU 1528 0.973 12.460 8.725 1.00 38.16 ATOM 512 CA LEU 1528 0.532 11.513 9.744 1.00 38.29 ATOM 513 CE LEU 1528 0.026 12.258 10.985 1.00 37.12 ATOM 514 CG LEU 1528 −0.505 11.412 12.153 1.00 39.03 ATOM 515 CD1 LEU 1528 0.499 10.323 12.539 1.00 35.39 ATOM 516 CD2 LEU 1528 −0.825 12.315 13.334 1.00 35.29 ATOM 517 C LEU 1528 −0.568 10.611 9.155 1.00 38.10 ATOM 518 O LEU 1528 −0.607 9.400 9.413 1.00 37.21 ATOM 519 N ILE 1529 −1.450 11.210 8.355 1.00 36.71 ATOM 521 CA ILE 1529 −2.531 10.472 7.718 1.00 35.93 ATOM 522 CB ILE 1529 −3.486 11.419 6.931 1.00 35.67 ATOM 523 CG2 ILE 1529 −4.492 10.619 6.119 1.00 34.04 ATOM 524 CG1 ILE 1529 −4.259 12.295 7.916 1.00 33.81 ATOM 525 CD1 ILE 1529 −5.177 13.288 7.276 1.00 33.58 ATOM 526 C ILE 1529 −1.912 9.447 6.786 1.00 37.49 ATOM 527 O ILE 1529 −2.274 8.269 6.829 1.00 37.11 ATOM 528 N SER 1530 −0.926 9.893 6.003 1.00 38.20 ATOM 530 CA SER 1530 −0.217 9.036 5.050 1.00 37.49 ATOM 531 CE SER 1530 0.911 9.822 4.370 1.00 43.32 ATOM 532 OG SER 1530 0.424 10.970 3.687 1.00 52.31 ATOM 534 C SER 1530 0.382 7.808 5.719 1.00 34.40 ATOM 535 O SER 1530 0.234 6.691 5.219 1.00 31.51 ATOM 536 N GLU 1531 1.048 8.028 6.851 1.00 32.08 ATOM 538 CA GLU 1531 1.690 6.952 7.594 1.00 30.60 ATOM 539 CE GLU 1531 2.506 7.515 8.759 1.00 29.70 ATOM 540 CG GLU 1531 3.094 6.428 9.657 1.00 30.53 ATOM 541 CD GLU 1531 3.871 6.962 10.839 1.00 33.17 ATOM 542 OE1 GLU 1531 4.473 6.134 11.552 1.00 33.38 ATOM 543 OE2 GLU 1531 3.883 8.193 11.062 1.00 37.52 ATOM 544 C GLU 1531 0.698 5.911 8.094 1.00 30.17 ATOM 545 O GLU 1531 0.991 4.714 8.100 1.00 29.76 ATOM 546 N MET 1532 −0.464 6.379 8.530 1.00 31.34 ATOM 548 CA MET 1532 −1.521 5.496 9.015 1.00 30.72 ATOM 549 CB MET 1532 −2.666 6.336 9.591 1.00 29.99 ATOM 550 CG MET 1532 −3.880 5.523 10.020 1.00 30.10 ATOM 551 SD MET 1532 −5.173 6.510 10.727 1.00 29.46 ATOM 552 CE MET 1532 −5.462 7.682 9.455 1.00 23.76 ATOM 553 C MET 1532 −2.025 4.638 7.843 1.00 30.47 ATOM 554 O MET 1532 −2.080 3.401 7.925 1.00 27.05 ATOM 555 N GLU 1533 −2.387 5.319 6.756 1.00 30.56 ATOM 557 CA GLU 1533 −2.863 4.674 5.542 1.00 30.56 ATOM 558 CE GLU 1533 −3.090 5.725 4.458 1.00 28.60 ATOM 559 CG GLU 1533 −4.226 6.677 4.761 1.00 29.08 ATOM 560 CD GLU 1533 −5.531 5.954 5.014 1.00 31.28 ATOM 561 OE1 GLU 1533 −6.006 5.230 4.117 1.00 33.09 ATOM 562 OE2 GLU 1533 −6.086 6.104 6.121 1.00 34.97 ATOM 563 C GLU 1533 −1.861 3.638 5.064 1.00 29.86 ATOM 564 O GLU 1533 −2.232 2.541 4.677 1.00 32.28 ATOM 565 N MET 1534 −0.590 4.014 5.107 1.00 32.54 ATOM 567 CA MET 1534 0.515 3.145 4.719 1.00 33.39 ATOM 568 CE MET 1534 1.826 3.894 4.885 1.00 34.70 ATOM 569 CG MET 1534 3.038 3.047 4.654 1.00 44.51 ATOM 570 SD MET 1534 3.479 3.063 2.943 1.00 52.81 ATOM 571 CE MET 1534 4.349 4.607 2.874 1.00 47.34 ATOM 572 C MET 1534 0.530 1.896 5.607 1.00 32.98 ATOM 573 O MET 1534 0.689 0.776 5.115 1.00 34.00 ATOM 574 N MET 1535 0.364 2.100 6.910 1.00 31.92 ATOM 576 CA MET 1535 0.336 0.986 7.848 1.00 30.80 ATOM 577 CE MET 1535 0.252 1.503 9.294 1.00 33.77 ATOM 578 CG MET 1535 1.509 2.216 9.810 1.00 32.26 ATOM 579 SD MET 1535 1.520 2.433 11.617 1.00 34.75 ATOM 580 CE MET 1535 1.183 4.173 11.723 1.00 37.86 ATOM 581 C MET 1535 −0.837 0.052 7.521 1.00 30.80 ATOM 582 O MET 1535 −0.704 −1.175 7.589 1.00 32.03 ATOM 583 N LYS 1536 −1.974 0.638 7.142 1.00 31.04 ATOM 585 CA LYS 1536 −3.170 −0.123 6.767 1.00 31.15 ATOM 586 CB LYS 1536 −4.334 0.808 6.415 1.00 31.21 ATOM 587 CG LYS 1536 −4.864 1.625 7.552 1.00 27.76 ATOM 588 CD LYS 1536 −5.973 2.540 7.103 1.00 21.44 ATOM 589 CE LYS 1536 −6.434 3.401 8.248 1.00 24.69 ATOM 590 NZ LYS 1536 −7.578 4.241 7.868 1.00 25.84 ATOM 594 C LYS 1536 −2.887 −1.003 5.561 1.00 30.71 ATOM 595 O LYS 1536 −3.238 −2.175 5.560 1.00 34.73 ATOM 596 N MET 1537 −2.309 −0.412 4.523 1.00 31.18 ATOM 598 CA MET 1537 −1.967 −1.148 3.307 1.00 31.53. ATOM 599 CB MET 1537 −1.370 −0.200 2.267 1.00 35.11 ATOM 600 CG MET 1537 −2.377 0.780 1.654 1.00 42.40 ATOM 601 SD MET 1537 −3.657 −0.051 0.685 1.00 50.10 ATOM 602 CE MET 1537 −3.069 0.266 −0.972 1.00 50.20 ATOM 603 C MET 1537 −0.976 −2.276 3.572 1.00 30.86 ATOM 604 O MET 1537 −1.218 −3.425 3.210 1.00 30.07 ATOM 605 N ILE 1538 0.119 −1.950 4.259 1.00 30.92 ATOM 607 CA ILE 1538 1.173 −2.923 4.563 1.00 28.12 ATOM 608 CB ILE 1538 2.359 −2.254 5.313 1.00 28.71 ATOM 609 CG2 ILE 1538 3.310 −3.303 5.865 1.00 29.72 ATOM 610 CG1 ILE 1538 3.126 −1.343 4.350 1.00 30.79 ATOM 611 CD1 ILE 1538 4.375 −0.745 4.945 1.00 32.46 ATOM 612 C ILE 1538 0.717 −4.179 5.299 1.00 26.33 ATOM 613 O ILE 1538 1.178 −5.276 4.996 1.00 24.20 ATOM 614 N GLY 1539 −0.188 −4.027 6.258 1.00 27.41 ATOM 616 CA GLY 1539 −0.651 −5.190 6.997 1.00 27.83 ATOM 617 C GLY 1539 0.240 −5.533 8.179 1.00 29.10 ATOM 618 O GLY 1539 1.308 −4.937 8.368 1.00 30.33 ATOM 619 N LYS 1540 −0.157 −6.561 8.916 1.00 29.46 ATOM 621 CA LYS 1540 0.539 −6.976 10.120 1.00 29.27 ATOM 622 CB LYS 1540 −0.470 −7.520 11.139 1.00 27.01 ATOM 623 CG LYS 1540 −1.438 −6.483 11.638 1.00 29.58 ATOM 624 CD LYS 1540 −2.496 −7.103 12.530 1.00 39.41 ATOM 625 CE LYS 1540 −3.548 −6.069 12.952 1.00 44.14 ATOM 626 NZ LYS 1540 −2.994 −4.996 13.828 1.00 46.92 ATOM 630 C LYS 1540 1.679 −7.962 10.020 1.00 27.17 ATOM 631 O LYS 1540 1.745 −8.794 9.111 1.00 26.20 ATOM 632 N HIS 1541 2.565 −7.856 11.006 1.00 26.96 ATOM 634 CA HIS 1541 3.690 −8.761 11.144 1.00 27.30 ATOM 635 CB HIS 1541 4.787 −8.506 10.120 1.00 22.20 ATOM 636 CO HIS 1541 5.849 −9.555 10.125 1.00 21.32 ATOM 637 CD2 HIS 1541 5.886 −10.789 9.555 1.00 23.29 ATOM 638 ND1 HIS 1541 7.052 −9.413 10.791 1.00 19.41 ATOM 640 CE1 HIS 1541 7.775 −10.509 10.633 1.00 23.61 ATOM 641 NE2 HIS 1541 7.097 −11.355 9.889 1.00 21.81 ATOM 643 C HIS 1541 4.245 −8.640 12.565 1.00 28.64 ATOM 644 O HIS 1541 4.290 −7.549 13.132 1.00 30.64 ATOM 645 N LYS 1542 4.650 −9.791 13.108 1.00 29.47 ATOM 647 CA LYS 1542 5.200 −9.893 14.457 1.00 28.78 ATOM 648 CB LYS 1542 5.683 −11.326 14.714 1.00 30.16 ATOM 649 CO LYS 1542 6.232 −11.572 16.112 1.00 32.63 ATOM 650 CD LYS 1542 5.277 −11.046 17.155 1.00 42.90 ATOM 651 CE LYS 1542 5.659 −11.475 18.551 1.00 48.13 ATOM 652 NZ LYS 1542 4.726 −10.930 19.564 1.00 54.87 ATOM 656 C LYS 1542 6.351 −8.928 14.705 1.00 26.54 ATOM 657 O LYS 1542 6.440 −8.321 15.773 1.00 26.19 ATOM 658 N ASN 1543 7.193 −8.733 13.697 1.00 24.36 ATOM 660 CA ASN 1543 8.357 −7.874 13.852 1.00 24.08 ATOM 661 CB ASN 1543 9.601 −8.596 13.359 1.00 22.69 ATOM 662 CG ASN 1543 9.781 −9.950 14.029 1.00 22.81 ATOM 663 OD1 ASN 1543 9.664 −10.996 13.388 1.00 23.62 ATOM 664 ND2 ASN 1543 10.028 −9.938 15.324 1.00 24.94 ATOM 667 C ASN 1543 8.318 −6.429 13.377 1.00 23.48 ATOM 668 O ASN 1543 9.351 −5.861 13.059 1.00 22.94 ATOM 669 N ILE 1544 7.130 −5.821 13.380 1.00 24.15 ATOM 671 CA ILE 1544 6.976 −4.407 13.012 1.00 24.60 ATOM 672 CE ILE 1544 6.516 −4.191 11.531 1.00 24.90 ATOM 673 CG2 ILE 1544 7.495 −4.852 10.571 1.00 21.57 ATOM 674 CG1 ILE 1544 5.081 −4.688 11.316 1.00 26.66 ATOM 675 CD1 ILE 1544 4.481 −4.321 9.945 1.00 23.98 ATOM 676 C ILE 1544 5.954 −3.785 13.955 1.00 24.78 ATOM 677 O ILE 1544 5.160 −4.503 14.558 1.00 27.87 ATOM 678 N ILE 1545 6.035 −2.474 14.159 1.00 26.39 ATOM 680 CA ILE 1545 5.089 −1.779 15.025 1.00 26.79 ATOM 681 CB ILE 1545 5.588 −0.345 15.384 1.00 28.85 ATOM 682 CG2 ILE 1545 4.512 0.449 16.103 1.00 23.60 ATOM 683 CG1 ILE 1545 6.833 −0.423 16.269 1.00 27.20 ATOM 684 CD1 ILE 1545 6.565 −0.990 17.639 1.00 27.12 ATOM 685 C ILE 1545 3.792 −1.708 14.224 1.00 26.99 ATOM 686 O ILE 1545 3.720 −1.023 13.197 1.00 27.61 ATOM 687 N ASN 1546 2.809 −2.495 14.654 1.00 26.70 ATOM 689 CA ASN 1546 1.514 −2.565 13.983 1.00 26.53 ATOM 690 CB ASN 1546 0.871 −3.953 14.169 1.00 26.23 ATOM 691 CO ASN 1546 1.695 −5.072 13.551 1.00 24.96 ATOM 692 OD1 ASN 1546 1.773 −5.206 12.330 1.00 28.08 ATOM 693 ND2 ASN 1546 2.319 −5.872 14.387 1.00 22.38 ATOM 696 C ASN 1546 0.521 −1.497 14.418 1.00 26.89 ATOM 697 O ASN 1546 0.610 −0.952 15.523 1.00 27.40 ATOM 698 N LEU 1547 −0.349 −1.138 13.481 1.00 27.77 ATOM 700 CA LEU 1547 −1.416 −0.175 13.701 1.00 28.28 ATOM 701 CB LEU 1547 −1.958 0.313 12.361 1.00 27.04 ATOM 702 CG LEU 1547 −3.199 1.194 12.408 1.00 25.74 ATOM 703 CD1 LEU 1547 −2.836 2.575 12.950 1.00 27.66 ATOM 704 CD2 LEU 1547 −3.799 1.289 11.014 1.00 23.38 ATOM 705 C LEU 1547 −2.498 −0.972 14.435 1.00 29.80 ATOM 706 O LEU 1547 −2.766 −2.135 14.105 1.00 28.63 ATOM 707 N LEU 1548 −3.088 −0.351 15.448 1.00 29.91 ATOM 709 CA LEU 1548 −4.114 −0.997 16.256 1.00 28.46 ATOM 710 CB LEU 1548 −3.735 −0.956 17.749 1.00 26.76 ATOM 711 CO LEU 1548 −2.460 −1.701 18.162 1.00 22.44 ATOM 712 CD1 LEU 1548 −2.277 −1.554 19.653 1.00 21.91 ATOM 713 CD2 LEU 1548 −2.551 −3.179 17.778 1.00 20.79 ATOM 714 C LEU 1548 −5.480 −0.365 16.058 1.00 27.31 ATOM 715 O LEU 1548 −6.489 −1.043 16.193 1.00 28.25 ATOM 716 N GLY 1549 −5.506 0.925 15.732 1.00 24.02 ATOM 718 CA GLY 1549 −6.774 1.598 15.553 1.00 24.57 ATOM 719 C GLY 1549 −6.548 3.077 15.395 1.00 25.19 ATOM 720 O GLY 1549 −5.400 3.488 15.231 1.00 28.77 ATOM 721 N ALA 1550 −7.617 3.875 15.427 1.00 24.66 ATOM 723 CA ALA 1550 −7.487 5.319 15.282 1.00 24.17 ATOM 724 CE ALA 1550 −7.206 5.680 13.824 1.00 24.29 ATOM 725 C ALA 1550 −8.695 6.103 15.765 1.00 23.95 ATOM 726 O ALA 1550 −9.810 5.590 15.780 1.00 24.95 ATOM 727 N CYS 1551 −8.444 7.336 16.199 1.00 25.03 ATOM 729 CA CYS 1551 −9.482 8.270 16.639 1.00 28.21 ATOM 730 CE CYS 1551 −9.221 8.774 18.055 1.00 26.76 ATOM 731 SG CYS 1551 −9.378 7.521 19.317 1.00 34.39 ATOM 732 C CYS 1551 −9.359 9.426 15.656 1.00 29.98 ATOM 733 O CYS 1551 −8.482 10.281 15.800 1.00 32.14 ATOM 734 N THR 1552 −10.198 9.412 14.625 1.00 31.09 ATOM 736 CA THR 1552 −10.135 10.435 13.595 1.00 32.91 ATOM 737 CB THR 1552 −10.052 9.781 12.189 1.00 32.60 ATOM 738 OG1 THR 1552 −11.276 9.097 11.890 1.00 32.12 ATOM 740 CG2 THR 1552 −8.928 8.768 12.144 1.00 32.74 ATOM 741 C THR 1552 −11.282 11.419 13.591 1.00 35.26 ATOM 742 O THR 1552 −11.171 12.525 13.057 1.00 35.10 ATOM 743 N GLN 1553 −12.397 11.014 14.179 1.00 39.01 ATOM 745 CA GLN 1553 −13.585 11.846 14.180 1.00 41.97 ATOM 746 CB GLN 1553 −14.832 10.968 14.020 1.00 41.17 ATOM 747 CG GLN 1553 −14.915 10.238 12.672 1.00 39.06 ATOM 748 CD GLN 1553 −14.900 11.200 11.496 1.00 41.84 ATOM 749 OE1 GLN 1553 −15.785 12.045 11.359 1.00 41.92 ATOM 750 NE2 GLN 1553 −13.876 11.090 10.652 1.00 42.33 ATOM 753 C GLN 1553 −13.727 12.777 15.372 1.00 45.35 ATOM 754 O GLN 1553 −13.358 12.423 16.489 1.00 47.02 ATOM 755 N ASP 1554 −14.225 13.981 15.090 1.00 48.60 ATOM 757 CA ASP 1554 −14.479 15.016 16.084 1.00 50.64 ATOM 758 CB ASP 1554 −15.832 14.766 16.758 1.00 54.52 ATOM 759 CG ASP 1554 −17.003 14.955 15.809 1.00 60.54 ATOM 760 OD1 ASP 1554 −18.072 15.409 16.274 1.00 66.04 ATOM 761 OD2 ASP 1554 −16.860 14.661 14.601 1.00 65.09 ATOM 762 C ASP 1554 −13.395 15.173 17.133 1.00 49.89 ATOM 763 O ASP 1554 −13.611 14.879 18.310 1.00 51.48 ATOM 764 N GLY 1555 −12.232 15.643 16.699 1.00 48.40 ATOM 766 CA GLY 1555 −11.131 15.834 17.617 1.00 46.16 ATOM 767 C GLY 1555 −9.798 15.626 16.935 1.00 44.64 ATOM 768 O GLY 1555 −9.737 15.581 15.716 1.00 45.22 ATOM 769 N PRO 1556 −8.708 15.525 17.702 1.00 44.68 ATOM 770 CD PRO 1556 −8.672 15.683 19.164 1.00 45.39 ATOM 771 CA PRO 1556 −7.359 15.326 17.177 1.00 42.95 ATOM 772 CB PRO 1556 −6.484 15.549 18.411 1.00 43.74 ATOM 773 CG PRO 1556 −7.354 16.347 19.345 1.00 47.32 ATOM 774 C PRO 1556 −7.164 13.912 16.665 1.00 42.34 ATOM 775 O PRO 1556 −7.636 12.953 17.287 1.00 42.75 ATOM 776 N LEU 1557 −6.451 13.788 15.547 1.00 39.83 ATOM 778 CA LEU 1557 −6.169 12.490 14.954 1.00 36.64 ATOM 779 CB LEU 1557 −5.496 12.669 13.587 1.00 34.49 ATOM 780 CG LEU 1557 −5.009 11.404 12.870 1.00 31.29 ATOM 781 CD1 LEU 1557 −6.169 10.436 12.628 1.00 27.86 ATOM 782 CD2 LEU 1557 −4.314 11.775 11.570 1.00 25.40. ATOM 783 C LEU 1557 −5.244 11.732 15.894 1.00 35.44 ATOM 784 O LEU 1557 −4.210 12.264 16.316 1.00 36.12 ATOM 785 N TYR 1558 −5.664 10.539 16.292 1.00 32.49 ATOM 787 CA TYR 1558 −4.861 9.697 17.157 1.00 31.87 ATOM 788 CB TYR 1558 −5.590 9.348 18.470 1.00 33.93 ATOM 789 CG TYR 1558 −5.695 10.476 19.471 1.00 35.34 ATOM 790 CD1 TYR 1558 −6.566 10.394 20.565 1.00 37.12 ATOM 791 CE1 TYR 1558 −6.683 11.456 21.479 1.00 36.44 ATOM 792 CD2 TYR 1558 −4.945 11.636 19.317 1.00 37.27 ATOM 793 CE2 TYR 1558 −5.054 12.690 20.213 1.00 39.62 ATOM 794 CZ TYR 1558 −5.921 12.598 21.289 1.00 40.05 ATOM 795 OH TYR 1558 −6.008 13.668 22.155 1.00 44.98 ATOM 797 C TYR 1558 −4.600 8.419 16.387 1.00 31.58 ATOM 798 O TYR 1558 −5.532 7.750 15.936 1.00 30.22 ATOM 799 N VAL 1559 −3.331 8.129 16.153 1.00 33.43 ATOM 801 CA VAL 1559 −2.947 6.907 15.463 1.00 31.42 ATOM 802 CB VAL 1559 −1.849 7.160 14.419 1.00 32.31 ATOM 803 CG1 VAL 1559 −1.516 5.851 13.675 1.00 26.79 ATOM 804 CG2 VAL 1559 −2.308 8.265 13.453 1.00 30.63 ATOM 805 C VAL 1559 −2.438 5.979 16.556 1.00 28.67 ATOM 806 O VAL 1559 −1.393 6.223 17.155 1.00 30.08 ATOM 807 N ILE 1560 −3.230 4.960 16.852 1.00 25.80 ATOM 809 CA ILE 1560 −2.915 3.998 17.894 1.00 25.33 ATOM 810 CB ILE 1560 −4.219 3.443 18.506 1.00 22.34 ATOM 811 CG2 ILE 1560 −3.931 2.695 19.784 1.00 20.36 ATOM 812 CG1 ILE 1560 −5.172 4.603 18.809 1.00 21.34 ATOM 813 CD1 ILE 1560 −6.583 4.190 19.093 1.00 20.68 ATOM 814 C ILE 1560 −2.073 2.857 17.341 1.00 27.16 ATOM 815 O ILE 1560 −2.520 2.116 16.455 1.00 29.67 ATOM 816 N VAL 1561 −0.858 2.714 17.860 1.00 27.69 ATOM 818 CA VAL 1561 0.060 1.667 17.411 1.00 28.27 ATOM 819 CB VAL 1561 1.311 2.269 16.696 1.00 27.34 ATOM 820 CG1 VAL 1561 0.892 3.019 15.445 1.00 21.76 ATOM 821 CG2 VAL 1561 2.074 3.201 17.639 1.00 26.00 ATOM 822 C VAL 1561 0.509 0.809 18.588 1.00 28.70 ATOM 823 O VAL 1561 0.221 1.139 19.746 1.00 30.52 ATOM 824 N GLU 1562 1.166 −0.311 18.286 1.00 28.64 ATOM 826 CA GLU 1562 1.658 −1.220 19.318 1.00 27.77 ATOM 827 CB GLU 1562 2.278 −2.465 18.693 1.00 24.57 ATOM 828 CG GLU 1562 1.251 −3.452 18.208 1.00 24.76 ATOM 829 CD GLU 1562 1.864 −4.641 17.501 1.00 27.27 ATOM 830 OE1 GLU 1562 1.272 −5.739 17.580 1.00 28.27 ATOM 831 OE2 GLU 1562 2.920 −4.487 16.849 1.00 29.25 ATOM 832 C GLU 1562 2.674 −0.538 20.217 1.00 28.79 ATOM 833 O GLU 1562 3.453 0.292 19.760 1.00 29.38 ATOM 834 N TYR 1563 2.627 −0.871 21.503 1.00 30.84 ATOM 836 CA TYR 1563 3.534 −0.304 22.493 1.00 31.43 ATOM 837 CB TYR 1563 2.782 −0.088 23.799 1.00 32.10 ATOM 838 CG TYR 1563 3.632 0.376 24.952 1.00 33.93 ATOM 839 CD1 TYR 1563 4.366 1.552 24.873 1.00 34.85 ATOM 840 CE1 TYR 1563 5.140 1.992 25.947 1.00 37.53 ATOM 841 CD2 TYR 1563 3.683 −0.356 26.136 1.00 34.81 ATOM 842 CE2 TYR 1563 4.452 0.072 27.211 1.00 34.01 ATOM 843 CZ TYR 1563 5.173 1.245 27.113 1.00 35.79 ATOM 844 OH TYR 1563 5.920 1.677 28.184 1.00 39.10 ATOM 846 C TYR 1563 4.767 −1.166 22.731 1.00 31.38 ATOM 847 O TYR 1563 4.672 −2.385 22.905 1.00 30.73 ATOM 848 N ALA 1564 5.930 −0.525 22.725 1.00 32.23 ATOM 850 CA ALA 1564 7.198 −1.212 22.953 1.00 35.90 ATOM 851 CB ALA 1564 8.178 −0.866 21.833 1.00 36.44 ATOM 852 C ALA 1564 7.711 −0.719 24.307 1.00 36.52 ATOM 853 O ALA 1564 8.332 0.349 24.403 1.00 39.16 ATOM 854 N SER 1565 7.424 −1.482 25.359 1.00 34.62 ATOM 856 CA SER 1565 7.801 −1.071 26.700 1.00 34.91 ATOM 857 CB SER 1565 7.124 −1.945 27.750 1.00 32.11 ATOM 858 OG SER 1565 7.606 −3.271 27.696 1.00 32.92 ATOM 860 C SER 1565 9.288 −0.968 26.996 1.00 35.56 ATOM 861 O SER 1565 9.674 −0.219 27.886 1.00 38.69 ATOM 862 N LYS 1566 10.127 −1.673 26.243 1.00 33.70 ATOM 864 CA LYS 1566 11.557 −1.625 26.526 1.00 31.40 ATOM 865 CB LYS 1566 12.137 −3.033 26.530 1.00 30.56 ATOM 866 CG LYS 1566 11.555 −3.869 27.664 1.00 32.32 ATOM 867 CD LYS 1566 11.997 −5.308 27.599 1.00 36.47 ATOM 868 CE LYS 1566 11.632 −6.031 28.872 1.00 36.97 ATOM 869 NZ LYS 1566 12.104 −7.436 28.804 1.00 41.62 ATOM 873 C LYS 1566 12.380 −0.664 25.683 1.00 32.18 ATOM 874 O LYS 1566 13.616 −0.691 25.715 1.00 32.57 ATOM 875 N GLY 1567 11.686 0.223 24.973 1.00 33.39 ATOM 877 CA GLY 1567 12.345 1.224 24.156 1.00 32.13 ATOM 878 C GLY 1567 13.074 0.719 22.928 1.00 31.70 ATOM 879 O GLY 1567 12.912 −0.430 22.530 1.00 33.30 ATOM 880 N ASN 1568 13.883 1.589 22.331 1.00 31.08 ATOM 882 CA ASN 1568 14.632 1.230 21.139 1.00 31.00 ATOM 883 CE ASN 1568 15.066 2.478 20.365 1.00 31.30 ATOM 884 CG ASN 1568 16.127 3.271 21.074 1.00 30.47 ATOM 885 OD1 ASN 1568 17.130 2.733 21.508 1.00 32.19 ATOM 886 ND2 ASN 1568 15.934 4.580 21.144 1.00 32.13 ATOM 889 C ASN 1568 15.802 0.295 21.393 1.00 30.62 ATOM 890 O ASN 1568 16.357 0.256 22.483 1.00 32.91 ATOM 891 N LEU 1569 16.193 −0.428 20.354 1.00 30.92 ATOM 893 CA LEU 1569 17.269 −1.403 20.417 1.00 31.22 ATOM 894 CE LEU 1569 17.418 −2.083 19.054 1.00 29.57 ATOM 895 CG LEU 1569 18.415 −3.231 18.893 1.00 29.22 ATOM 896 CD1 LEU 1569 18.284 −4.261 20.024 1.00 21.30 ATOM 897 CD2 LEU 1569 18.184 −3.863 17.523 1.00 24.99 ATOM 898 C LEU 1569 18.609 −0.838 20.878 1.00 32.44 ATOM 899 O LEU 1569 19.328 −1.499 21.618 1.00 33.12 ATOM 900 N ARG 1570 18.954 0.370 20.432 1.00 33.24 ATOM 902 CA ARG 1570 20.218 0.983 20.834 1.00 33.01 ATOM 903 CE ARG 1570 20.348 2.394 20.256 1.00 32.36 ATOM 904 CG ARG 1570 21.586 3.129 20.758 1.00 38.28 ATOM 905 CD ARG 1570 21.672 4.538 20.221 1.00 41.93 ATOM 906 NE ARG 1570 20.428 5.278 20.412 1.00 49.82 ATOM 908 CZ ARG 1570 19.975 5.721 21.584 1.00 52.37 ATOM 909 NH1 ARG 1570 20.659 5.510 22.712 1.00 51.61 ATOM 912 NH2 ARG 1570 18.824 6.377 21.622 1.00 53.28 ATOM 915 C ARG 1570 20.308 1.023 22.371 1.00 33.90 ATOM 916 O ARG 1570 21.184 0.391 22.970 1.00 33.17 ATOM 917 N GLU 1571 19.359 1.730 22.981 1.00 33.45 ATOM 919 CA GLU 1571 19.284 1.861 24.432 1.00 34.87 ATOM 920 CE GLU 1571 18.052 2.688 24.794 1.00 35.83 ATOM 921 CG GLU 1571 18.158 4.145 24.354 1.00 41.61 ATOM 922 CD GLU 1571 16.814 4.870 24.318 1.00 47.33 ATOM 923 OE1 GLU 1571 15.759 4.199 24.362 1.00 50.68 ATOM 924 OE2 GLU 1571 16.812 6.120 24.218 1.00 48.07 ATOM 925 C GLU 1571 19.223 0.487 25.098 1.00 34.39 ATOM 926 O GLU 1571 19.968 0.202 26.041 1.00 34.04 ATOM 927 N TYR 1572 18.363 −0.376 24.572 1.00 33.49 ATOM 929 CA TYR 1572 18.204 −1.728 25.083 1.00 30.45 ATOM 930 CE TYR 1572 17.210 −2.495 24.202 1.00 28.13 ATOM 931 CG TYR 1572 17.074 −3.971 24.487 1.00 25.80 ATOM 932 CD1 TYR 1572 16.105 −4.443 25.371 1.00 28.92 ATOM 933 CE1 TYR 1572 15.954 −5.804 25.618 1.00 30.03 ATOM 934 CD2 TYR 1572 17.899 −4.899 23.863 1.00 24.61 ATOM 935 CE2 TYR 1572 17.760 −6.260 24.102 1.00 26.05 ATOM 936 CZ TYR 1572 16.790 −6.705 24.982 1.00 29.23 ATOM 937 OH TYR 1572 16.651 −8.052 25.227 1.00 33.74 ATOM 939 C TYR 1572 19.549 −2.447 25.113 1.00 31.30 ATOM 940 O TYR 1572 19.880 −3.126 26.090 1.00 32.43 ATOM 941 N LEU 1573 20.334 −2.266 24.058 1.00 29.68 ATOM 943 CA LEU 1573 21.625 −2.923 23.972 1.00 30.04 ATOM 944 CE LEU 1573 22.145 −2.909 22.529 1.00 26.13 ATOM 945 CG LEU 1573 21.532 −3.870 21.490 1.00 25.24 ATOM 946 CD1 LEU 1573 22.097 −3.563 20.113 1.00 19.70 ATOM 947 CD2 LEU 1573 21.807 −5.317 21.839 1.00 22.05 ATOM 948 C LEU 1573 22.645 −2.308 24.927 1.00 34.47 ATOM 949 O LEU 1573 23.354 −3.031 25.644 1.00 34.95 ATOM 950 N GLN 1574 22.691 −0.980 24.978 1.00 35.47 ATOM 952 CA GLN 1574 23.639 −0.293 25.850 1.00 37.09 ATOM 953 CE GLN 1574 23.601 1.206 25.579 1.00 36.70 ATOM 954 CG GLN 1574 24.033 1.559 24.171 1.00 39.77 ATOM 955 CD GLN 1574 23.960 3.045 23.884 1.00 41.51 ATOM 956 OE1 GLN 1574 23.592 3.837 24.751 1.00 42.57 ATOM 957 NE2 GLN 1574 24.288 3.431 22.652 1.00 41.34 ATOM 960 C GLN 1574 23.400 −0.588 27.332 1.00 37.85 ATOM 961 O GLN 1574 24.343 −0.801 28.090 1.00 38.87 ATOM 962 N ALA 1575 22.131 −0.667 27.720 1.00 39.01 ATOM 964 CA ALA 1575 21.740 −0.944 29.098 1.00 37.00 ATOM 965 CB ALA 1575 20.261 −0.678 29.273 1.00 35.71 ATOM 966 C ALA 1575 22.061 −2.359 29.559 1.00 39.14 ATOM 967 O ALA 1575 21.839 −2.692 30.719 1.00 43.81 ATOM 968 N ARG 1576 22.563 −3.201 28.665 1.00 38.39 ATOM 970 CA ARG 1576 22.897 −4.568 29.032 1.00 37.71 ATOM 971 CB ARG 1576 21.994 −5.544 28.290 1.00 38.26 ATOM 972 CG ARG 1576 20.555 −5.383 28.700 1.00 38.00 ATOM 973 CD ARG 1576 19.653 −6.282 27.920 1.00 34.74 ATOM 974 NE ARG 1576 18.279 −6.190 28.388 1.00 32.88 ATOM 976 CZ ARG 1576 17.572 −5.066 28.442 1.00 34.02 ATOM 977 NH1 ARG 1576 18.114 −3.913 28.068 1.00 35.57 ATOM 980 NH2 ARG 1576 16.298 −5.102 28.800 1.00 36.71 ATOM 983 C ARG 1576 24.365 −4.927 28.828 1.00 39.59 ATOM 984 O ARG 1576 24.735 −6.113 28.788 1.00 39.83 ATOM 985 N ARG 1577 25.200 −3.900 28.687 1.00 38.82 ATOM 987 CA ARG 1577 26.631 −4.101 28.520 1.00 39.07 ATOM 988 CE ARG 1577 27.310 −2.797 28.090 1.00 34.91 ATOM 989 CG ARG 1577 27.033 −2.323 26.681 1.00 33.87 ATOM 990 CD ARG 1577 27.730 −0.981 26.428 1.00 33.06 ATOM 991 NE ARG 1577 27.722 −0.612 25.015 1.00 38.87 ATOM 993 CZ ARG 1577 28.174 0.538 24.517 1.00 39.76 ATOM 994 NH1 ARG 1577 28.683 1.470 25.305 1.00 40.68 ATOM 997 NH2 ARG 1577 28.122 0.758 23.213 1.00 43.26 ATOM 1000 C ARG 1577 27.181 −4.501 29.885 1.00 41.58 ATOM 1001 O ARG 1577 26.586 −4.181 30.917 1.00 42.48 ATOM 1002 N PRO 1578 28.294 −5.249 29.919 1.00 43.07 ATOM 1003 CD PRO 1578 29.110 −5.812 28.823 1.00 43.36 ATOM 1004 CA PRO 1578 28.839 −5.626 31.223 1.00 42.69 ATOM 1005 CE PRO 1578 29.966 −6.595 30.857 1.00 42.22 ATOM 1006 CG PRO 1578 30.412 −6.103 29.516 1.00 43.64 ATOM 1007 C PRO 1578 29.366 −4.350 31.882 1.00 43.37 ATOM 1008 O PRO 1578 29.530 −3.319 31.215 1.00 42.50 ATOM 1009 N PRO 1579 29.596 −4.380 33.198 1.00 45.24 ATOM 1010 CD PRO 1579 29.279 −5.435 34.174 1.00 44.69 ATOM 1011 CA PRO 1579 30.099 −3.187 33.882 1.00 46.27 ATOM 1012 CB PRO 1579 29.979 −3.567 35.353 1.00 45.78 ATOM 1013 CG PRO 1579 28.894 −4.615 35.361 1.00 46.15 ATOM 1014 C PRO 1579 31.548 −2.869 33.500 1.00 48.38 ATOM 1015 O PRO 1579 32.410 −3.753 33.478 1.00 50.64 ATOM 1016 N GLU 1592 19.022 −5.398 32.495 1.00 65.98 ATOM 1018 CA GLU 1592 20.442 −5.048 32.492 1.00 64.80 ATOM 1019 CB GLU 1592 20.796 −4.241 33.740 1.00 67.30 ATOM 1020 C GLU 1592 21.351 −6.275 32.371 1.00 63.80 ATOM 1021 O GLU 1592 22.545 −6.149 32.089 1.00 65.21 ATOM 1022 N GLU 1593 20.789 −7.458 32.607 1.00 61.44 ATOM 1024 CA GLU 1593 21.560 −8.691 32.495 1.00 60.82 ATOM 1025 CE GLU 1593 20.681 −9.899 32.807 1.00 61.47 ATOM 1026 C GLU 1593 22.144 −8.803 31.089 1.00 59.12 ATOM 1027 O GLU 1593 21.468 −8.525 30.097 1.00 59.49 ATOM 1028 N GLN 1594 23.408 −9.201 31.017 1.00 57.33 ATOM 1030 CA GLN 1594 24.103 −9.334 29.744 1.00 55.30 ATOM 1031 CE GLN 1594 25.523 −9.880 29.957 1.00 54.87 ATOM 1032 CG GLN 1594 26.438 −8.959 30.757 1.00 53.34 ATOM 1033 CD GLN 1594 27.704 −9.660 31.248 1.00 55.27 ATOM 1034 OE1 GLN 1594 28.256 −10.536 30.572 1.00 56.47 ATOM 1035 NE2 GLN 1594 28.166 −9.275 32.434 1.00 51.46 ATOM 1038 C GLN 1594 23.336 −10.229 28.781 1.00 52.29 ATOM 1039 O GLN 1594 22.648 −11.166 29.190 1.00 52.56 ATOM 1040 N LEU 1595 23.447 −9.913 27.499 1.00 49.40 ATOM 1042 CA LEU 1595 22.783 −10.676 26.455 1.00 46.00 ATOM 1043 CB LEU 1595 22.452 −9.760 25.274 1.00 42.94 ATOM 1044 CG LEU 1595 21.390 −8.711 25.626 1.00 43.90 ATOM 1045 CD1 LEU 1595 21.495 −7.484 24.743 1.00 39.46 ATOM 1046 CD2 LEU 1595 20.005 −9.347 25.569 1.00 41.86 ATOM 1047 C LEU 1595 23.741 −11.762 26.029 1.00 43.96 ATOM 1048 O LEU 1595 24.950 −11.550 26.043 1.00 44.24 ATOM 1049 N SER 1596 23.217 −12.941 25.714 1.00 43.29 ATOM 1051 CA SER 1596 24.076 −14.027 25.275 1.00 42.40 ATOM 1052 CE SER 1596 23.388 −15.374 25.484 1.00 41.83 ATOM 1053 OG SER 1596 22.218 −15.483 24.697 1.00 44.25 ATOM 1055 C SER 1596 24.392 −13.817 23.800 1.00 42.64 ATOM 1056 O SER 1596 23.857 −12.900 23.171 1.00 43.14 ATOM 1057 N SER 1597 25.277 −14.645 23.255 1.00 42.59 ATOM 1059 CA SER 1597 25.629 −14.553 21.850 1.00 42.91 ATOM 1060 CE SER 1597 26.739 −15.547 21.516 1.00 45.26 ATOM 1061 OG SER 1597 27.812 −15.436 22.431 1.00 56.41 ATOM 1063 C SER 1597 24.380 −14.909 21.048 1.00 42.35 ATOM 1064 O SER 1597 24.113 −14.322 20.003 1.00 43.71 ATOM 1065 N LYS 1598 23.621 −15.881 21.544 1.00 40.61 ATOM 1067 CA LYS 1598 22.405 −16.298 20.867 1.00 38.61 ATOM 1068 CE LYS 1598 21.848 −17.575 21.483 1.00 36.33 ATOM 1069 CG LYS 1598 21.135 −18.439 20.468 1.00 40.09 ATOM 1070 CD LYS 1598 20.213 −19.434 21.118 1.00 43.39 ATOM 1071 CE LYS 1598 19.766 −20.494 20.122 1.00 48.25 ATOM 1072 NZ LYS 1598 20.930 −21.290 19.623 1.00 50.46 ATOM 1076 C LYS 1598 21.348 −15.194 20.895 1.00 38.17 ATOM 1077 O LYS 1598 20.579 −15.053 19.945 1.00 41.27 ATOM 1078 N ASP 1599 21.321 −14.408 21.969 1.00 35.90 ATOM 1080 CA ASP 1599 20.366 −13.307 22.099 1.00 34.08 ATOM 1081 CE ASP 1599 20.450 −12.661 23.477 1.00 37.83 ATOM 1082 CG ASP 1599 19.822 −13.505 24.562 1.00 39.93 ATOM 1083 ODi ASP 1599 20.089 −13.217 25.742 1.00 45.85 ATOM 1084 0D2 ASP 1599 19.060 −14.444 24.240 1.00 41.06 ATOM 1085 C ASP 1599 20.634 −12.243 21.061 1.00 32.37 ATOM 1086 O ASP 1599 19.704 −11.701 20.466 1.00 32.58 ATOM 1087 N LEU 1600 21.915 −11.945 20.873 1.00 30.45 ATOM 1089 CA LEU 1600 22.355 −10.948 19.902 1.00 29.59 ATOM 1090 CE LEU 1600 23.841 −10.654 20.097 1.00 28.59 ATOM 1091 CG LEU 1600 24.238 −10.057 21.449 1.00 24.59 ATOM 1092 CD1 LEU 1600 25.747 −9.869 21.522 1.00 18.40 ATOM 1093 CD2 LEU 1600 23.529 −8.745 21.626 1.00 21.71 ATOM 1094 C LEU 1600 22.073 −11.393 18.458 1.00 28.54 ATOM 1095 O LEU 1600 21.578 −10.613 17.648 1.00 25.59 ATOM 1096 N VAL 1601 22.377 −12.645 18.134 1.00 29.13 ATOM 1098 CA VAL 1601 22.111 −13.154 16.793 1.00 29.74 ATOM 1099 CE VAL 1601 22.780 −14.513 16.551 1.00 29.63 ATOM 1100 CG1 VAL 1601 22.615 −14.922 15.105 1.00 29.30 ATOM 1101 CG2 VAL 1601 24.259 −14.422 16.873 1.00 28.52 ATOM 1102 C VAL 1601 20.591 −13.247 16.564 1.00 29.98 ATOM 1103 O VAL 1601 20.106 −13.040 15.452 1.00 29.73 ATOM 1104 N SER 1602 19.855 −13.493 17.645 1.00 30.97 ATOM 1106 CA SER 1602 18.399 −13.576 17.607 1.00 29.64 ATOM 1107 CE SER 1602 17.894 −14.141 18.925 1.00 30.45 ATOM 1108 OG SER 1602 16.483 −14.158 18.962 1.00 39.63 ATOM 1110 C SER 1602 17.784 −12.192 17.343 1.00 29.30 ATOM 1111 O SER 1602 16.772 −12.071 16.641 1.00 28.74 ATOM 1112 N CYS 1603 18.385 −11.157 17.925 1.00 27.68 ATOM 1114 CA CYS 1603 17.931 −9.783 17.717 1.00 27.32 ATOM 1115 CB CYS 1603 18.791 −8.790 18.516 1.00 25.40 ATOM 1116 SG CYS 1603 18.472 −7.039 18.177 0.50 20.76 PRT1 ATOM 1117 C CYS 1603 18.057 −9.468 16.225 1.00 28.34 ATOM 1118 O CYS 1603 17.134 −8.926 15.629 1.00 29.70 ATOM 1119 N ALA 1604 19.192 −9.837 15.627 1.00 29.36 ATOM 1121 CA ALA 1604 19.438 −9.601 14.195 1.00 28.78 ATOM 1122 CB ALA 1604 20.861 −10.066 13.808 1.00 22.61 ATOM 1123 C ALA 1604 18.386 −10.304 13.324 1.00 30.14 ATOM 1124 O ALA 1604 17.792 −9.690 12.426 1.00 31.64 ATOM 1125 N TYR 1605 18.156 −11.587 13.605 1.00 29.84 ATOM 1127 CA TYR 1605 17.179 −12.392 12.874 1.00 28.26 ATOM 1128 CB TYR 1605 17.107 −13.789 13.488 1.00 28.74 ATOM 1129 CG TYR 1605 16.018 −14.673 12.912 1.00 31.12 ATOM 1130 CD1 TYR 1605 16.152 −15.256 11.650 1.00 32.53 ATOM 1131 CE1 TYR 1605 15.144 −16.067 11.121 1.00 30.84 ATOM 1132 CD2 TYR 1605 14.853 −14.926 13.634 1.00 31.21 ATOM 1133 CE2 TYR 1605 13.850 −15.734 13.116 1.00 29.69 ATOM 1134 CZ TYR 1605 14.002 −16.296 11.864 1.00 30.82 ATOM 1135 OH TYR 1605 12.990 −17.069 11.359 1.00 33.77 ATOM 1137 C TYR 1605 15.788 −11.758 12.853 1.00 27.33 ATOM 1138 O TYR 1605 15.152 −11.691 11.805 1.00 27.94 ATOM 1139 N GLN 1606 15.323 −11.292 14.007 1.00 27.93 ATOM 1141 CA GLN 1606 14.008 −10.659 14.115 1.00 27.20 ATOM 1142 CB GLN 1606 13.686 −10.335 15.570 1.00 26.40 ATOM 1143 CO GLN 1606 13.301 −11.556 16.402 1.00 28.12 ATOM 1144 CD GLN 1606 13.114 −11.215 17.865 1.00 30.41 ATOM 1145 OE1 GLN 1606 12.188 −10.489 18.234 1.00 34.34 ATOM 1146 NE2 GLN 1606 14.008 −11.701 18.700 1.00 31.44 ATOM 1149 C GLN 1606 13.906 −9.397 13.275 1.00 29.67 ATOM 1150 O GLN 1606 12.884 −9.148 12.622 1.00 30.74 ATOM 1151 N VAL 1607 14.970 −8.602 13.281 1.00 29.59 ATOM 1153 CA VAL 1607 14.996 −7.377 12.501 1.00 27.00 ATOM 1154 CB VAL 1607 16.235 −6.544 12.842 1.00 27.20 ATOM 1155 CO1 VAL 1607 16.382 −5.397 11.859 1.00 28.11 ATOM 1156 CO2 VAL 1607 16.113 −5.996 14.266 1.00 24.79 ATOM 1157 C VAL 1607 14.966 −7.725 11.014 1.00 28.02 ATOM 1158 O VAL 1607 14.229 −7.108 10.241 1.00 28.28 ATOM 1159 N ALA 1608 15.736 −8.741 10.626 1.00 27.56 ATOM 1161 CA ALA 1608 15.787 −9.206 9.236 1.00 27.36 ATOM 1162 CB ALA 1608 16.801 −10.339 9.095 1.00 26.25 ATOM 1163 C ALA 1608 14.402 −9.674 8.779 1.00 28.58 ATOM 1164 O ALA 1608 14.013 −9.446 7.624 1.00 29.11 ATOM 1165 N ARG 1609 13.660 −10.326 9.680 1.00 28.88 ATOM 1167 CA ARG 1609 12.306 −10.797 9.376 1.00 27.17 ATOM 1168 CB ARG 1609 11.797 −11.731 10.464 1.00 29.68 ATOM 1169 CO ARG 1609 12.458 −13.062 10.439 1.00 31.65 ATOM 1170 CD ARG 1609 11.612 −14.049 11.177 1.00 38.21 ATOM 1171 NE ARG 1609 10.856 −14.897 10.269 1.00 41.10 ATOM 1173 CZ ARG 1609 10.048 −15.872 10.667 1.00 41.97 ATOM 1174 NH1 ARG 1609 9.886 −16.125 11.959 1.00 40.69 ATOM 1177 NH2 ARG 1609 9.411 −16.609 9.770 1.00 43.57 ATOM 1180 C ARG 1609 11.312 −9.654 9.183 1.00 25.38 ATOM 1181 O ARG 1609 10.480 −9.693 8.260 1.00 25.75 ATOM 1182 N GLY 1610 11.365 −8.661 10.070 1.00 24.03 ATOM 1184 CA GLY 1610 10.480 −7.517 9.939 1.00 21.74 ATOM 1185 C GLY 1610 10.734 −6.864 8.592 1.00 23.32 ATOM 1186 O GLY 1610 9.805 −6.540 7.850 1.00 23.39 ATOM 1187 N MET 1611 12.016 −6.714 8.265 1.00 24.48 ATOM 1189 CA MET 1611 12.453 −6.125 7.002 1.00 23.13 ATOM 1190 CB MET 1611 13.949 −5.860 7.035 1.00 19.46 ATOM 1191 CG MET 1611 14.339 −4.671 7.910 1.00 22.46 ATOM 1192 SD MET 1611 13.457 −3.123 7.536 1.00 25.27 ATOM 1193 CE MET 1611 13.900 −2.801 5.876 1.00 22.25 ATOM 1194 C MET 1611 12.100 −7.005 5.811 1.00 24.87 ATOM 1195 O MET 1611 11.699 −6.497 4.755 1.00 24.09 ATOM 1196 N GLU 1612 12.230 −8.321 5.975 1.00 25.48 ATOM 1198 CA GLU 1612 11.894 −9.232 4.890 1.00 25.42 ATOM 1199 CB GLU 1612 12.155 −10.691 5.288 1.00 23.41 ATOM 1200 CG GLU 1612 11.664 −11.679 4.232 1.00 25.14 ATOM 1201 CD GLU 1612 11.872 −13.141 4.599 1.00 28.60 ATOM 1202 OE1 GLU 1612 11.637 −13.514 5.777 1.00 30.10 ATOM 1203 OE2 GLU 1612 12.244 −13.928 3.694 1.00 29.53 ATOM 1204 C GLU 1612 10.418 −9.021 4.521 1.00 26.92 ATOM 1205 O GLU 1612 10.065 −8.928 3.343 1.00 29.61 ATOM 1206 N TYR 1613 9.576 −8.884 5.542 1.00 27.88 ATOM 1208 CA TYR 1613 8.154 −8.675 5.337 1.00 23.82 ATOM 1209 CB TYR 1613 7.415 −8.769 6.667 1.00 24.17 ATOM 1210 CG TYR 1613 5.941 −8.492 6.545 1.00 23.73 ATOM 1211 CD1 TYR 1613 5.064 −9.483 6.096 1.00 22.17 ATOM 1212 CE1 TYR 1613 3.698 −9.235 5.965 1.00 21.08 ATOM 1213 CD2 TYR 1613 5.419 −7.237 6.865 1.00 23.16 ATOM 1214 CE2 TYR 1613 4.054 −6.976 6.736 1.00 26.38 ATOM 1215 CZ TYR 1613 3.200 −7.981 6.287 1.00 23.16 ATOM 1216 OH TYR 1613 1.855 −7.725 6.149 1.00 25.50 ATOM 1218 C TYR 1613 7.885 −7.327 4.670 1.00 23.17 ATOM 1219 O TYR 1613 7.147 −7.246 3.689 1.00 24.21 ATOM 1220 N LEU 1614 8.481 −6.266 5.206 1.00 23.04 ATOM 1222 CA LEU 1614 8.316 −4.920 4.652 1.00 21.81 ATOM 1223 CE LEU 1614 9.107 −3.906 5.484 1.00 19.94 ATOM 1224 CG LEU 1614 8.609 −3.616 6.902 1.00 21.94 ATOM 1225 CD1 LEU 1614 9.580 −2.719 7.654 1.00 14.28 ATOM 1226 CD2 LEU 1614 7.227 −2.977 6.814 1.00 17.45 ATOM 1227 C LEU 1614 8.764 −4.858 3.182 1.00 23.74 ATOM 1228 O LEU 1614 8.169 −4.150 2.367 1.00 25.26 ATOM 1229 N ALA 1615 9.831 −5.587 2.862 1.00 25.00 ATOM 1231 CA ALA 1615 10.357 −5.644 1.502 1.00 23.04 ATOM 1232 CB ALA 1615 11.710 −6.360 1.483 1.00 20.02 ATOM 1233 C ALA 1615 9.351 −6.357 0.605 1.00 23.15 ATOM 1234 O ALA 1615 9.076 −5.891 −0.503 1.00 25.25 ATOM 1235 N SER 1616 8.754 −7.441 1.104 1.00 23.64 ATOM 1237 CA SER 1616 7.758 −8.199 0.337 1.00 23.60 ATOM 1238 CE SER 1616 7.346 −9.453 1.107 1.00 22.46 ATOM 1239 OG SER 1616 6.531 −9.131 2.224 1.00 26.66 ATOM 1241 C SER 1616 6.505 −7.369 0.025 1.00 25.45 ATOM 1242 O SER 1616 5.813 −7.607 −0.967 1.00 26.67 ATOM 1243 N LYS 1617 6.193 −6.436 0.916 1.00 25.47 ATOM 1245 CA LYS 1617 5.051 −5.551 0.781 1.00 25.04 ATOM 1246 CE LYS 1617 4.513 −5.183 2.163 1.00 26.30 ATOM 1247 CG LYS 1617 3.778 −6.318 2.851 1.00 28.58 ATOM 1248 CD LYS 1617 2.438 −6.530 2.169 1.00 33.00 ATOM 1249 CE LYS 1617 1.652 −7.676 2.764 1.00 38.57 ATOM 1250 NZ LYS 1617 2.167 −8.987 2.300 1.00 45.15 ATOM 1254 C LYS 1617 5.417 −4.293 0.002 1.00 26.34 ATOM 1255 O LYS 1617 4.649 −3.336 −0.034 1.00 26.77 ATOM 1256 N LYS 1618 6.592 −4.319 −0.632 1.00 27.17 ATOM 1258 CA LYS 1618 7.084 −3.197 −1.447 1.00 28.20 ATOM 1259 CE LYS 1618 6.053 −2.819 −2.528 1.00 28.42 ATOM 1260 CG LYS 1618 5.971 −3.749 −3.730 1.00 26.63 ATOM 1261 CD LYS 1618 5.573 −5.163 −3.364 1.00 30.45 ATOM 1262 CE LYS 1618 5.636 −6.087 −4.570 1.00 32.50 ATOM 1263 NZ LYS 1618 4.621 −5.729 −5.600 1.00 34.89 ATOM 1267 C LYS 1618 7.466 −1.951 −0.643 1.00 28.78 ATOM 1268 O LYS 1618 7.556 −0.848 −1.199 1.00 28.78 ATOM 1269 N CYS 1619 7.753 −2.130 0.646 1.00 29.26 ATOM 1271 CA CYS 1619 8.111 −1.022 1.522 1.00 28.32 ATOM 1272 CB CYS 1619 7.391 −1.173 2.873 1.00 26.33 ATOM 1273 SG CYS 1619 7.754 0.105 4.136 1.00 27.82 ATOM 1274 C CYS 1619 9.622 −0.841 1.728 1.00 29.15 ATOM 1275 O CYS 1619 10.336 −1.786 2.072 1.00 29.55 ATOM 1276 N ILE 1620 10.096 0.378 1.457 1.00 29.39 ATOM 1278 CA ILE 1620 11.502 0.761 1.625 1.00 27.44 ATOM 1279 CB ILE 1620 12.030 1.543 0.381 1.00 25.37 ATOM 1280 CG2 ILE 1620 13.521 1.806 0.506 1.00 19.80 ATOM 1281 CG1 ILE 1620 11.767 0.764 −0.913 1.00 25.40 ATOM 1282 CD1 ILE 1620 12.100 1.557 −2.164 1.00 27.51 ATOM 1283 C ILE 1620 11.553 1.686 2.855 1.00 26.56 ATOM 1284 O ILE 1620 11.011 2.792 2.833 1.00 26.68 ATOM 1285 N HIS 1621 12.193 1.210 3.916 1.00 26.31 ATOM 1287 CA HIS 1621 12.297 1.967 5.162 1.00 25.00 ATOM 1288 CB HIS 1621 13.081 1.174 6.210 1.00 23.08 ATOM 1289 CG HIS 1621 12.848 1.633 7.618 1.00 23.21 ATOM 1290 CD2 HIS 1621 12.224 1.027 8.656 1.00 22.69 ATOM 1291 ND1 HIS 1621 13.260 2.862 8.088 1.00 25.34. ATOM 1293 CE1 HIS 1621 12.909 2.993 9.356 1.00 24.18 ATOM 1294 NE2 HIS 1621 12.273 1.891 9.719 1.00 25.86 ATOM 1296 C HIS 1621 12.963 3.316 4.976 1.00 25.09 ATOM 1297 O HIS 1621 12.408 4.328 5.349 1.00 28.21 ATOM 1298 N ARG 1622 14.162 3.315 4.402 1.00 26.09 ATOM 1300 CA ARG 1622 14.976 4.520 4.183 1.00 26.50 ATOM 1301 CB ARG 1622 14.180 5.670 3.558 1.00 23.52 ATOM 1302 CG ARG 1622 13.673 5.326 2.202 1.00 23.81 ATOM 1303 CD ARG 1622 12.995 6.494 1.551 1.00 28.42 ATOM 1304 NE ARG 1622 12.677 6.170 0.180 1.00 32.52 ATOM 1306 CZ ARG 1622 11.623 5.455 −0.197 1.00 32.34 ATOM 1307 NH1 ARG 1622 10.774 4.994 0.711 1.00 30.07 ATOM 1310 NH2 ARG 1622 11.460 5.138 −1.489 1.00 28.30 ATOM 1313 C ARG 1622 15.740 4.993 5.423 1.00 26.31 ATOM 1314 O ARG 1622 16.698 5.757 5.313 1.00 26.19 ATOM 1315 N ASP 1623 15.379 4.495 6.596 1.00 27.41 ATOM 1317 CA ASP 1623 16.114 4.879 7.788 1.00 29.94 ATOM 1318 CB ASP 1623 15.562 6.155 8.430 1.00 34.83 ATOM 1319 CG ASP 1623 16.481 6.689 9.533 1.00 38.84 ATOM 1320 OD1 ASP 1623 15.971 7.265 10.514 1.00 44.51 ATOM 1321 OD2 ASP 1623 17.721 6.514 9.423 1.00 37.59 ATOM 1322 C ASP 1623 16.203 3.763 8.812 1.00 28.71 ATOM 1323 O ASP 1623 15.845 3.927 9.990 1.00 26.21 ATOM 1324 N LEU 1624 16.735 2.633 8.357 1.00 26.82 ATOM 1326 CA LEU 1624 16.905 1.469 9.216 1.00 25.91 ATOM 1327 CB LEU 1624 17.025 0.209 8.367 1.00 23.35 ATOM 1328 CG LEU 1624 17.089 −1.107 9.127 1.00 21.09 ATOM 1329 CD1 LEU 1624 15.824 −1.303 10.009 1.00 1.4.44 ATOM 1330 CD2 LEU 1624 17.282 −2.215 8.101 1.00 18.30 ATOM 1331 C LEU 1624 18.136 1.640 10.105 1.00 24.93 ATOM 1332 O LEU 1624 19.235 1.897 9.611 1.00 25.58 ATOM 1333 N ALA 1625 17.912 1.557 11.416 1.00 26.30 ATOM 1335 CA ALA 1625 18.945 1.702 12.445 1.00 23.59 ATOM 1336 CB ALA 1625 19.271 3.174 12.654 1.00 15.82 ATOM 1337 C ALA 1625 18.351 1.116 13.732 1.00 23.64 ATOM 1338 O ALA 1625 17.135 0.928 13.825 1.00 26.66 ATOM 1339 N ALA 1626 19.197 0.815 14.712 1.00 21.59 ATOM 1341 CA ALA 1626 18.708 0.266 15.974 1.00 21.66 ATOM 1342 CB ALA 1626 19.860 −0.179 16.838 1.00 22.97 ATOM 1343 C ALA 1626 17.835 1.272 16.731 1.00 24.98 ATOM 1344 O ALA 1626 17.072 0.891 17.620 1.00 26.84 ATOM 1345 N ARG 1627 17.978 2.558 16.409 1.00 24.55 ATOM 1347 CA ARG 1627 17.178 3.598 17.042 1.00 25.29 ATOM 1348 CB ARG 1627 17.699 4.983 16.673 1.00 26.66 ATOM 1349 CG ARG 1627 17.675 5.276 15.179 1.00 30.56 ATOM 1350 CD ARG 162.7 18.033 6.715 14.902 1.00 34.97 ATOM 1351 NE ARG 1627 18.177 6.980 13.470 1.00 40.03 ATOM 1353 CZ ARG 1627 19.322 6.864 12.809 1.00 40.62 ATOM 1354 NH1 ARG 1627 20.421 6.485 13.441 1.00 46.52 ATOM 1357 NH2 ARG 1627 19.377 7.159 11.523 1.00 43.25 ATOM 1360 C ARG 1627 15.739 3.472 16.542 1.00 27.33 ATOM 1361 O ARG 1627 14.804 3.895 17.210 1.00 28.14 ATOM 1362 N ASN 1628 15.576 2.894 15.353 1.00 27.46 ATOM 1364 CA ASN 1628 14.260 2.716 14.757 1.00 28.07 ATOM 1365 CB ASN 1628 14.254 3.178 13.304 1.00 31.54 ATOM 1366 CG ASN 1628 14.307 4.690 13.172 1.00 35.35 ATOM 1367 OD1 ASN 1628 13.538 5.405 13.824 1.00 37.63 ATOM 1368 ND2 ASN 1628 15.221 5.184 12.354 1.00 32.95 ATOM 1371 C ASN 1628 13.733 1.301 14.880 1.00 27.69 ATOM 1372 O ASN 1628 12.896 0.864 14.082 1.00 28.10 ATOM 1373 N VAL 1629 14.247 0.580 15.870 1.00 26.21 ATOM 1375 CA VAL 1629 13.817 −0.775 16.169 1.00 25.90 ATOM 1376 CB VAL 1629 14.926 −1.812 15.946 1.00 24.73 ATOM 1377 CG1 VAL 1629 14.480 −3.151 16.499 1.00 19.90 ATOM 1378 CG2 VAL 1629 15.274 −1.924 14.440 1.00 18.28 ATOM 1379 C VAL 1629 13.470 −0.732 17.646 1.00 27.81 ATOM 1380 O VAL 1629 14.313 −0.404 18.468 1.00 29.18 ATOM 1381 N LEU 1630 12.212 −0.987 17.976 1.00 30.36 ATOM 1383 CA LEU 1630 11.776 −0.950 19.365 1.00 31.04 ATOM 1384 CB LEU 1630 10.471 −0.151 19.489 1.00 31.93 ATOM 1385 CG LEU 1630 10.441 1.211 18.784 1.00 27.43 ATOM 1386 CD1 LEU 1630 9.126 1.879 19.009 1.00 23.21 ATOM 1387 CD2 LEU 1630 11.564 2.093 19.271 1.00 28.21 ATOM 1388 C LEU 1630 11.625 −2.356 19.935 1.00 31.58 ATOM 1389 O LEU 1630 11.415 −3.321 19.195 1.00 33.03 ATOM 1390 N VAL 1631 11.752 −2.467 21.253 1.00 31.30 ATOM 1392 CA VAL 1631 11.660 −3.749 21.937 1.00 30.60 ATOM 1393 CB VAL 1631 12.964 −4.027 22.745 1.00 29.35 ATOM 1394 CG1 VAL 1631 12.995 −5.469 23.243 1.00 23.92 ATOM 1395 CG2 VAL 1631 14.197 −3.714 21.895 1.00 24.26 ATOM 1396 C VAL 1631 10.450 −3.773 22.885 1.00 32.64 ATOM 1397 O VAL 1631 10.198 2.821 23.643 1.00 33.01 ATOM 1398 N THR 1632 9.697 −4.863 22.827 1.00 34.45 ATOM 1400 CA THR 1632 8.516 −5.035 23.660 1.00 34.29 ATOM 1401 CB THR 1632 7.466 −5.941 22.962 1.00 34.62 ATOM 1402 OG1 THR 1632 7.965 −7.288 22.881 1.00 34.40 ATOM 1404 CG2 THR 1632 7.154 −5.414 21.551 1.00 31.61 ATOM 1405 C THR 1632 8.896 −5.678 24.989 1.00 35.41 ATOM 1406 O THR 1632 10.002 −6.189 25.146 1.00 34.79 ATOM 1407 N GLU 1633 7.939 −5.706 25.913 1.00 36.86 ATOM 1409 CA GLU 1633 8.156 −6.298 27.224 1.00 37.27 ATOM 1410 CB GLU 1633 6.893 −6.182 28.079 1.00 37.66 ATOM 1411 CG GLU 1633 7.031 −6.718 29.514 1.00 44.43 ATOM 1412 CD GLU 1633 8.048 −5.959 30.378 1.00 46.68 ATOM 1413 OE1 GLU 1633 8.104 −4.708 30.300 1.00 49.88 ATOM 1414 OE2 GLU 1633 8.783 −6.612 31.156 1.00 48.53 ATOM 1415 C GLU 1633 8.561 −7.753 27.088 1.00 37.15 ATOM 1416 O GLU 1633 9.227 −8.292 27.954 1.00 38.60 ATOM 1417 N ASP 1634 8.167 −8.384 25.990 1.00 38.41 ATOM 1419 CA ASP 1634 8.505 −9.787 25.770 1.00 38.86 ATOM 1420 CB ASP 1634 7.381 −10.499 25.013 1.00 44.27 ATOM 1421 CG ASP 1634 6.022 −10.349 25.690 1.00 50.18 ATOM 1422 OD1 ASP 1634 5.726 −11.141 26.617 1.00 52.07 ATOM 1423 OD2 ASP 1634 5.253 −9.439 25.295 1.00 50.17 ATOM 1424 C ASP 1634 9.804 −9.947 25.007 1.00 36.23 ATOM 1425 O ASP 1634 10.141 −11.049 24.608 1.00 35.82 ATOM 1426 N ASN 1635 10.528 −8.851 24.799 1.00 36.51 ATOM 1428 CA ASN 1635 11.795 −8.864 24.052 1.00 37.41 ATOM 1429 CB ASN 1635 12.801 −9.842 24.678 1.00 38.49 ATOM 1430 CG ASN 1635 13.343 −9.359 26.003 1.00 37.71 ATOM 1431 OD1 ASN 1635 13.499 −8.156 26.227 1.00 38.09 ATOM 1432 ND2 ASN 1635 13.679 −10.300 26.874 1.00 39.63 ATOM 1435 C ASN 1635 11.655 −9.162 22.552 1.00 36.37 ATOM 1436 O ASN 1635 12.522 −9.811 21.944 1.00 36.41 ATOM 1437 N VAL 1636 10.547 −8.721 21.966 1.00 33.79 ATOM 1439 CA VAL 1636 10.315 −8.910 20.543 1.00 30.59 ATOM 1440 CB VAL 1636 8.820 −9.139 20.218 1.00 28.83 ATOM 1441 CG1 VAL 1636 8.615 −9.182 18.712 1.00 26.13 ATOM 1442 CG2 VAL 1636 8.339 −10.431 20.838 1.00 25.67 ATOM 1443 C VAL 1636 10.782 −7.630 19.863 1.00 30.18 ATOM 1444 O VAL 1636 10.436 −6.527 20.301 1.00 27.86 ATOM 1445 N MET 1637 11.609 −7.792 18.832 1.00 30.93 ATOM 1447 CA MET 1637 12.140 −6.679 18.060 1.00 28.34 ATOM 1448 CB MET 1637 13.397 −7.138 17.330 1.00 30.84 ATOM 1449 CG MET 1637 14.480 −7.693 18.254 1.00 30.73 ATOM 1450 SD MET 1637 15.050 −6.490 19.477 1.00 32.20 ATOM 1451 CE MET 1637 15.074 −7.500 20.938 1.00 28.71 ATOM 1452 C MET 1637 11.082 −6.264 17.051 1.00 27.29 ATOM 1453 O MET 1637 10.587 −7.099 16.297 1.00 27.32 ATOM 1454 N LYS 1638 10.733 −4.983 17.045 1.00 27.19 ATOM 1456 CA LYS 1638 9.716 −4.450 16.143 1.00 26.38 ATOM 1457 CB LYS 1638 8.437 −4.120 16.912 1.00 27.09 ATOM 1458 CG LYS 1638 7.702 −5.351 17.407 1.00 29.71 ATOM 1459 CD LYS 1638 6.386 −5.018 18.109 1.00 31.48 ATOM 1460 CE LYS 1638 5.485 −6.263 18.202 1.00 27.09 ATOM 1461 NZ LYS 1638 4.888 −6.561 16.869 1.00 26.68 ATOM 1465 C LYS 1638 10.196 −3.208 15.416 1.00 26.56 ATOM 1466 O LYS 1638 10.514 −2.194 16.040 1.00 27.40 ATOM 1467 N ILE 1639 10.211 −3.271 14.092 1.00 24.31 ATOM 1469 CA ILE 1639 10.649 −2.147 13.289 1.00 24.84 ATOM 1470 CB ILE 1639 10.924 −2.588 11.836 1.00 25.81 ATOM 1471 CG2 ILE 1639 11.248 −1.395 10.952 1.00 24.18 ATOM 1472 CG1 ILE 1639 12.094 −3.566 11.826 1.00 25.01 ATOM 1473 CD1 ILE 1639 12.075 −4.499 10.675 1.00 27.90 ATOM 1474 C ILE 16.39 9.641 −0.999 13.348 1.00 24.90 ATOM 1475 O ILE 1639 8.435 −1.186 13.170 1.00 25.24 ATOM 1476 N ALA 1640 10.167 0.183 13.163 1.00 25.70 ATOM 1478 CA ALA 1640 9.378 1.392 13.744 1.00 27.61 ATOM 1479 CB ALA 1640 9.699 2.094 15.070 1.00 26.37 ATOM 1480 C ALA 1640 9.637 2.348 12.576 1.00 28.35 ATOM 1481 O ALA 1640 10.650 2.243 11.871 1.00 28.40 ATOM 1482 N ASP 1641 8.676 3.237 12.354 1.00 29.74 ATOM 1484 CA ASP 1641 8.760 4.272 11.325 1.00 32.13 ATOM 1485 CB ASP 1641 9.873 5.273 11.688 1.00 34.31 ATOM 1486 CG ASP 1641 9.507 6.158 12.896 1.00 36.31 ATOM 1487 OD1 ASP 1641 10.299 7.056 13.258 1.00 42.18 ATOM 1488 OD2 ASP 1641 8.420 5.974 13.483 1.00 41.03 ATOM 1489 C ASP 1641 8.882 3.840 9.867 1.00 32.00 ATOM 1490 O ASP 1641 9.339 4.617 9.021 1.00 32.65 ATOM 1491 N PHE 1642 8.415 2.634 9.563 1.00 30.61 ATOM 1493 CA PHE 1642 8.473 2.119 8.200 1.00 30.06 ATOM 1494 CB PHE 1642 8.248 0.606 8.189 1.00 24.46 ATOM 1495 CG PHE 1642 6.981 0.176 8.854 1.00 23.26 ATOM 1496 CD1 PHE 1642 5.799 0.075 8.125 1.00 19.66 ATOM 1497 CD2 PHE 1642 6.966 −0.134 10.209 1.00 22.88 ATOM 1498 CE1 PHE 1642 4.609 −0.331 8.734 1.00 20.97 ATOM 1499 CE2 PHE 1642 5.785 −0.540 10.830 1.00 26.61 ATOM 1500 CZ PHE 1642 4.599 −0.639 10.083 1.00 24.82 ATOM 1501 C PHE 1642 7.512 2.830 7.225 1.00 33.14 ATOM 1502 O PHE 1642 7.791 2.922 6.029 1.00 36.48 ATOM 1503 N GLY 1643 6.411 3.372 7.741 1.00 32.65 ATOM 1505 CA GLY 1643 5.462 4.059 6.876 1.00 32.28 ATOM 1506 C GLY 1643 5.629 5.560 6.913 1.00 32.19 ATOM 1507 O GLY 1643 4.795 6.310 6.415 1.00 30.74 ATOM 1508 N LEU 1644 6.739 5.997 7.486 1.00 36.80 ATOM 1510 CA LEU 1644 7.052 7.406 7.630 1.00 41.95 ATOM 1511 CB LEU 1644 8.332 7.551 8.439 1.00 37.41 ATOM 1512 CG LEU 1644 8.377 8.746 9.369 1.00 38.98 ATOM 1513 CD1 LEU 1644 7.384 8.548 10.493 1.00 40.45 ATOM 1514 CD2 LEU 1644 9.775 8.904 9.929 1.00 41.94 ATOM 1515 C LEU 1644 7.189 8.150 6.296 1.00 47.55 ATOM 1516 O LEU 1644 7.787 7.648 5.341 1.00 50.55 ATOM 1517 N ALA 1645 6.637 9.356 6.247 1.00 52.59 ATOM 1519 CA ALA 1645 6.686 10.194 5.055 1.00 56.88 ATOM 1520 CB ALA 1645 5.391 10.999 4.942 1.00 58.01 ATOM 1521 C ALA 1645 7.880 11.135 5.178 1.00 58.95 ATOM 1522 O ALA 1645 8.064 11.770 6.224 1.00 59.37 ATOM 1523 N ARG 1646 8.700 11.211 4.133 1.00 60.26 ATOM 1525 CA ARG 1646 9.870 12.088 4.165 1.00 63.04 ATOM 1526 CB ARG 1646 10.995 11.444 4.976 1.00 64.92 ATOM 1527 C ARG 1646 10.377 12.461 2.782 1.00 63.84 ATOM 1528 O ARG 1646 10.361 11.641 1.864 1.00 63.55 ATOM 1529 N ASP 1647 10.801 13.714 2.633 1.00 65.18 ATOM 1531 CA ASP 1647 11.332 14.190 1.361 1.00 67.26 ATOM 1532 CB ASP 1647 10.989 15.670 1.150 1.00 68.92 ATOM 1533 CG ASP 1647 11.164 16.124 −0.304 1.00 70.88 ATOM 1534 OD1 ASP 1647 12.196 15.811 −0.943 1.00 70.33 ATOM 1535 OD2 ASP 1647 10.258 16.825 −0.808 1.00 71.39 ATOM 1536 C ASP 1647 12.847 14.005 1.405 1.00 68.40 ATOM 1537 O ASP 1647 13.545 14.711 2.142 1.00 68.66 ATOM 1538 N ILE 1648 13.347 13.055 0.621 1.00 68.48 ATOM 1540 CA ILE 1648 14.777 12.773 0.570 1.00 69.00 ATOM 1541 CB ILE 1648 15.091 11.535 −0.314 1.00 66.28 ATOM 1542 CG2 ILE 1648 14.231 10.352 0.131 1.00 65.14 ATOM 1543 CG1 ILE 1648 14.869 11.853 −1.799 1.00 63.01 ATOM 1544 CD1 ILE 1648 15.274 10.746 −2.738 1.00 60.11 ATOM 1545 C ILE 1648 15.542 13.990 0.046 1.00 71.12 ATOM 1546 O ILE 1648 16.628 14.310 0.525 1.00 72.41 ATOM 1547 N HIS 1649 14.923 14.710 −0.883 1.00 73.09 ATOM 1549 CA HIS 1649 15.546 15.890 −1.469 1.00 74.66 ATOM 1550 CB HIS 1649 14.921 16.191 −2.835 1.00 76.00 ATOM 1551 CG HIS 1649 15.178 15.157 −3.867 1.00 78.03 ATOM 1552 CD2 HIS 1649 16.314 14.425 −4.151 1.00 78.85 ATOM 1553 ND1 HIS 1649 14.245 14.739 −4.795 1.00 78.49 ATOM 1555 CE1 HIS 1649 14.765 13.835 −5.584 1.00 78.94 ATOM 1556 NE2 HIS 1649 16.005 13.623 −5.226 1.00 78.22 ATOM 1558 C HIS 1649 15.466 17.108 −0.549 1.00 75.04 ATOM 1559 O HIS 1649 15.567 18.244 −1.007 1.00 75.49 ATOM 1560 N HIS 1650 15.265 16.860 0.743 1.00 76.11 ATOM 1562 CA HIS 1650 15.181 17.918 1.748 1.00 77.63 ATOM 1563 CB HIS 1650 13.723 18.327 1.995 1.00 81.10 ATOM 1564 CG HIS 1650 13.206 19.352 1.033 1.00 86.06 ATOM 1565 CD2 HIS 1650 13.662 20.592 0.730 1.00 88.74 ATOM 1566 ND1 HIS 1650 12.099 19.146 0.239 1.00 88.83 ATOM 1568 CE1 HIS 1650 11.893 20.211 −0.511 1.00 90.51 ATOM 1569 NE2 HIS 1650 12.823 21.103 −0.238 1.00 90.75 ATOM 1571 C HIS 1650 15.824 17.482 3.064 1.00 77.39 ATOM 1572 O HIS 1650 15.651 18.133 4.091 1.00 77.42 ATOM 1573 N ILE 1651 16.573 16.385 3.024 1.00 77.73 ATOM 1575 CA ILE 1651 17.241 15.864 4.212 1.00 77.02 ATOM 1576 CB ILE 1651 17.788 14.433 3.974 1.00 78.24 ATOM 1577 CG2 ILE 1651 18.647 13.963 5.153 1.00 77.92 ATOM 1578 CG1 ILE 1651 16.633 13.458 3.750 1.00 80.90 ATOM 1579 CD1 ILE 1651 17.094 12.032 3.483 1.00 82.41 ATOM 1580 C ILE 1651 18.411 16.748 4.620 1.00 76.15 ATOM 1581 O ILE 1651 19.269 17.078 3.803 1.00 76.52 ATOM 1582 N ASP 1652 18.432 17.150 5.882 1.00 75.13 ATOM 1584 CA ASP 1652 19.527 17.957 6.384 1.00 73.91 ATOM 1585 CB ASP 1652 19.068 18.781 7.592 1.00 76.30 ATOM 1586 CG ASP 1652 20.216 19.499 8.286 1.00 79.91 ATOM 1587 OD1 ASP 1652 21.247 19.786 7.636 1.00 82.38 ATOM 1588 OD2 ASP 1652 20.081 19.780 9.497 1.00 81.51 ATOM 1589 C ASP 1652 20.637 16.984 6.783 1.00 72.31 ATOM 1590 O ASP 1652 20.599 16.403 7.866 1.00 71.41 ATOM 1591 N TYR 1653 21.610 16.805 5.894 1.00 71.44 ATOM 1593 CA TYR 1653 22.736 15.900 6.143 1.00 70.07 ATOM 1594 CB TYR 1653 23.655 15.849 4.921 1.00 66.96 ATOM 1595 CG TYR 1653 23.153 14.932 3.834 1.00 66.43 ATOM 1596 CD1 TYR 1653 23.881 14.757 2.657 1.00 66.60 ATOM 1597 CE1 TYR 1653 23.434 13.898 1.653 1.00 68.33 ATOM 1598 CD2 TYR 1653 21.960 14.224 3.981 1.00 66.58 ATOM 1599 CE2 TYR 1653 21.500 13.363 2.990 1.00 68.84 ATOM 1600 CZ TYR 1653 22.241 13.205 1.823 1.00 69.34 ATOM 1601 OH TYR 1653 21.781 12.360 0.833 1.00 69.88 ATOM 1603 C TYR 1653 23.557 16.227 7.391 1.00 70.80 ATOM 1604 O TYR 1653 24.197 15.351 7.975 1.00 70.62 ATOM 1605 N TYR 1654 23.531 17.488 7.802 1.00 70.76 ATOM 1607 CA TYR 1654 24.280 17.902 8.972 1.00 70.97 ATOM 1608 CB TYR 1654 24.795 19.328 8.783 1.00 69.27 ATOM 1609 CG TYR 1654 25.935 19.401 7.787 1.00 69.68 ATOM 1610 CD1 TYR 1654 25.696 19.352 6.415 1.00 69.51 ATOM 1611 CE1 TYR 1654 26.750 19.380 5.498 1.00 70.15 ATOM 1612 CD2 TYR 1654 27.256 19.482 8.221 1.00 69.92 ATOM 1613 CE2 TYR 1654 28.314 19.513 7.316 1.00 70.26 ATOM 1614 CZ TYR 1654 28.057 19.462 5.958 1.00 70.22 ATOM 1615 OH TYR 1654 29.111 19.492 5.069 1.00 69.67 ATOM 1617 C TYR 1654 23.503 17.763 10.272 1.00 72.19 ATOM 1618 O TYR 1654 24.035 18.043 11.344 1.00 73.21 ATOM 1619 N LYS 1655 22.269 17.275 10.183 1.00 73.05 ATOM 1621 CA LYS 1655 21.424 17.108 11.363 1.00 74.81 ATOM 1622 CB LYS 1655 19.955 17.124 10.953 1.00 75.63 ATOM 1623 CG LYS 1655 18.978 17.239 12.102 1.00 79.16 ATOM 1624 CD LYS 1655 17.581 17.513 11.576 1.00 84.09 ATOM 1625 CE LYS 1655 16.517 17.244 12.634 1.00 87.56 ATOM 1626 NZ LYS 1655 15.139 17.478 12.097 1.00 89.36 ATOM 1630 C LYS 1655 21.738 15.834 12.156 1.00 75.72 ATOM 1631 O LYS 1655 21.900 14.751 11.586 1.00 77.14 ATOM 1632 N LYS 1656 21.815 15.977 13.477 1.00 75.08 ATOM 1634 CA LYS 1656 22.106 14.857 14.363 1.00 73.36 ATOM 1635 CB LYS 1656 23.062 15.296 15.477 1.00 72.88 ATOM 1636 CG LYS 1656 24.475 15.599 15.007 1.00 72.87 ATOM 1637 CD LYS 1656 25.346 16.048 16.167 1.00 74.66 ATOM 1638 CE LYS 1656 26.830 15.945 15.828 1.00 74.84 ATOM 1639 NZ LYS 1656 27.701 16.322 16.981 1.00 73.74 ATOM 1643 C LYS 1656 20.827 14.311 14.982 1.00 72.45 ATOM 1644 O LYS 1656 19.795 14.991 15.007 1.00 72.74 ATOM 1645 N THR 1657 20.900 13.075 15.469 1.00 71.26 ATOM 1647 CA THR 1657 19.763 12.426 16.107 1.00 70.05 ATOM 1648 CB THR 1657 19.969 10.886 16.206 1.00 68.30 ATOM 1649 OG1 THR 1657 21.084 10.598 17.060 1.00 69.34 ATOM 1651 CG2 THR 1657 20.244 10.292 14.839 1.00 66.16 ATOM 1652 C THR 1657 19.707 13.019 17.504 1.00 70.37 ATOM 1653 O THR 1657 20.608 13.761 17.892 1.00 71.47 ATOM 1654 N THR 1658 18.669 12.691 18.263 1.00 70.80 ATOM 1656 CA THR 1658 18.559 13.205 19.626 1.00 71.54 ATOM 1657 CB THR 1658 17.334 12.600 20.325 1.00 71.20 ATOM 1658 C THR 1658 19.844 12.865 20.394 1.00 70.91 ATOM 1659 O THR 1658 20.429 13.722 21.063 1.00 71.25 ATOM 1660 N ASN 1659 20.331 11.639 20.199 1.00 68.87 ATOM 1662 CA ASN 1659 21.537 11.157 20.871 1.00 65.52 ATOM 1663 CB ASN 1659 21.602 9.635 20.796 1.00 67.39 ATOM 1664 CG ASN 1659 22.419 9.032 21.916 1.00 69.42 ATOM 1665 OD1 ASN 1659 22.261 9.410 23.076 1.00 71.70. ATOM 1666 ND2 ASN 1659 23.278 8.069 21.583 1.00 68.93 ATOM 1669 C ASN 1659 22.830 11.749 20.318 1.00 62.51 ATOM 1670 O ASN 1659 23.917 11.351 20.733 1.00 61.47 ATOM 1671 N GLY 1660 22.706 12.654 19.348 1.00 59.76 ATOM 1673 CA GLY 1660 23.859 13.307 18.750 1.00 57.70 ATOM 1674 C GLY 1660 24.553 12.593 17.597 1.00 56.98 ATOM 1675 O GLY 1660 25.659 12.979 17.199 1.00 57.55 ATOM 1676 N ARG 1661 23.909 11.573 17.037 1.00 55.34 ATOM 1678 CA ARG 1661 24.504 10.826 15.928 1.00 52.28 ATOM 1679 CB ARG 1661 24.255 9.334 16.092 1.00 50.68 ATOM 1680 CG ARG 1661 24.811 8.744 17.365 1.00 49.61 ATOM 1681 CD ARG 1661 24.542 7.267 17.361 1.00 52.30 ATOM 1682 NE ARG 1661 24.942 6.599 18.595 1.00 53.64 ATOM 1684 CZ ARG 1661 24.731 5.306 18.826 1.00 56.32 ATOM 1685 NH1 ARG 1661 24.124 4.559 17.901 1.00 54.04 ATOM 1688 NH2 ARG 1661 25.145 4.754 19.965 1.00 54.48 ATOM 1691 C ARG 1661 24.015 11.288 14.560 1.00 49.89 ATOM 1692 O ARG 1661 22.916 11.812 14.429 1.00 51.43 ATOM 1693 N LEU 1662 24.839 11.080 13.542 1.00 45.78 ATOM 1695 CA LEU 1662 24.503 11.481 12.186 1.00 43.05 ATOM 1696 CE LEU 1662 25.762 12.020 11.492 1.00 42.15 ATOM 1697 CG LEU 1662 26.351 13.306 12.088 1.00 40.60 ATOM 1698 CD1 LEU 1662 27.780 13.512 11.641 1.00 38.14 ATOM 1699 CD2 LEU 1662 25.484 14.499 11.705 1.00 42.00 ATOM 1700 C LEU 1662 23.867 10.346 11.370 1.00 41.81 ATOM 1701 O LEU 1662 24.548 9.406 10.957 1.00 40.46 ATOM 1702 N PRO 1663 22.546 10.428 11.118 1.00 40.49 ATOM 1703 CD PRO 1663 21.659 11.519 11.561 1.00 40.60 ATOM 1704 CA PRO 1663 21.794 9.423 10.351 1.00 38.17 ATOM 1705 CE PRO 1663 20.433 10.095 10.158 1.00 38.43 ATOM 1706 CG PRO 1663 20.282 10.901 11.414 1.00 40.65 ATOM 1707 C PRO 1663 22.445 9.059 9.012 1.00 35.40 ATOM 1708 O PRO 1663 22.265 7.949 8.521 1.00 33.01 ATOM 1709 N VAL 1664 23.200 9.989 8.426 1.00 34.56 ATOM 1711 CA VAL 1664 23.889 9.722 7.160 1.00 32.91 ATOM 1712 CE VAL 1664 24.757 10.916 6.659 1.00 33.13 ATOM 1713 CG1 VAL 1664 23.912 11.929 5.968 1.00 33.44 ATOM 1714 CG2 VAL 1664 25.521 11.554 7.792 1.00 33.68 ATOM 1715 C VAL 1664 24.812 8.511 7.266 1.00 30.58 ATOM 1716 O VAL 1664 25.157 7.903 6.257 1.00 29.20 ATOM 1717 N LYS 1665 25.211 8.171 8.489 1.00 28.02 ATOM 1719 CA LYS 1665 26.102 7.044 8.726 1.00 24.95 ATOM 1720 CB LYS 1665 26.749 7.153 10.098 1.00 24.39 ATOM 1721 CG LYS 1665 27.811 8.231 10.140 1.00 28.36 ATOM 1722 CD LYS 1665 28.189 8.628 11.548 1.00 29.24 ATOM 1723 CE LYS 1665 29.269 9.690 11.489 1.00 31.15 ATOM 1724 NZ LYS 1665 29.639 10.194 12.836 1.00 35.47 ATOM 1728 C LYS 1665 25.440 5.692 8.543 1.00 25.16 ATOM 1729 O LYS 1665 26.096 4.671 8.627 1.00 24.34 ATOM 1730 N TRP 1666 24.138 5.698 8.286 1.00 25.16 ATOM 1732 CA TRP 1666 23.414 4.461 8.053 1.00 26.61 ATOM 1733 CB TRP 1666 22.157 4.412 8.917 1.00 28.17 ATOM 1734 CG TRP 1666 22.428 3.931 10.330 1.00 30.26 ATOM 1735 CD2 TRP 1666 22.930 4.714 11.426 1.00 26.92 ATOM 1736 CE2 TRP 1666 23.063 3.837 12.537 1.00 26.34 ATOM 1737 CE3 TRP 1666 23.286 6.057 11.598 1.00 24.69 ATOM 1738 CD1 TRP 1666 22.276 2.656 10.800 1.00 26.44 ATOM 1739 NE1 TRP 1666 22.659 2.592 12.118 1.00 25.65 ATOM 1741 CZ2 TRP 1666 23.535 4.264 13.779 1.00 24.97 ATOM 1742 CZ3 TRP 1666 23.758 6.484 12.837 1.00 22.23 ATOM 1743 CH2 TRP 1666 23.877 5.587 13.908 1.00 24.97 ATOM 1744 C TRP 1666 23.048 4.345 6.572 1.00 27.24 ATOM 1745 O TRP 1666 22.573 3.301 6.116 1.00 29.16 ATOM 1746 N MET 1667 23.355 5.390 5.811 1.00 26.70 ATOM 1748 CA MET 1667 23.022 5.444 4.398 1.00 25.21 ATOM 1749 CB MET 1667 22.828 6.893 3.963 1.00 28.81 ATOM 1750 CG MET 1667 21.704 7.630 4.637 1.00 35.42 ATOM 1751 SD MET 1667 21.567 9.283 3.924 1.00 42.64 ATOM 1752 CE MET 1667 20.959 8.858 2.369 1.00 41.32 ATOM 1753 C MET 1667 23.984 4.807 3.417 1.00 25.03 ATOM 1754 O MET 1667 25.182 5.047 3.446 1.00 24.24 ATOM 1755 N ALA 1668 23.420 4.034 2.501 1.00 26.70 ATOM 1757 CA ALA 1668 24.186 3.398 1.441 1.00 27.82 ATOM 1758 CB ALA 1668 23.272 2.509 0.601 1.00 25.36 ATOM 1759 C ALA 1668 24.738 4.528 0.575 1.00 28.42 ATOM 1760 O ALA 1668 24.044 5.521 0.321 1.00 27.52 ATOM 1761 N PRO 1669 25.972 4.374 0.065 1.00 28.95 ATOM 1762 CD PRO 1669 26.867 3.214 0.170 1.00 27.98 ATOM 1763 CA PRO 1669 26.571 5.418 −0.775 1.00 28.76 ATOM 1764 CB PRO 1669 27.814 4.731 −1.326 1.00 28.58 ATOM 1765 CG PRO 1669 28.193 3.809 −0.209 1.00 30.22 ATOM 1766 C PRO 1669 25.647 5.909 −1.893 1.00 27.08 ATOM 1767 O PRO 1669 25.496 7.107 −2.093 1.00 28.31 ATOM 1768 N GLU 1670 24.993 4.997 −2.595 1.00 25.42 ATOM 1770 CA GLU 1670 24.110 5.423 −3.673 1.00 27.02 ATOM 1771 CB GLU 1670 23.680 4.233 −4.542 1.00 27.18 ATOM 1772 CG GLU 1670 22.662 3.294 −3.911 1.00 27.66 ATOM 1773 CD GLU 1670 23.280 2.162 −3.112 1.00 27.75 ATOM 1774 OE1 GLU 1670 22.488 1.309 −2.647 1.00 27.12 ATOM 1775 OE2 GLU 1670 24.526 2.114 −2.944 1.00 21.64 ATOM 1776 C GLU 1670 22.896 6.229 −3.189 1.00 26.88 ATOM 1777 O GLU 1670 22.348 7.037 −3.929 1.00 24.52 ATOM 1778 N ALA 1671 22.477 6.009 −1.948 1.00 29.43 ATOM 1780 CA ALA 1671 21.342 6.744 −1.392 1.00 29.29 ATOM 1781 CB ALA 1671 20.751 5.989 −0.217 1.00 26.98 ATOM 1782 C ALA 1671 21.826 8.124 −0.939 1.00 31.14 ATOM 1783 O ALA 1671 21.159 9.135 −1.143 1.00 31.67 ATOM 1784 N LEU 1672 23.013 8.139 −0.343 1.00 32.31 ATOM 1786 CA LEU 1672 23.636 9.352 0.154 1.00 33.79 ATOM 1787 CB LEU 1672 24.841 8.986 1.008 1.00 34.49 ATOM 1788 CG LEU 1672 25.585 10.166 1.618 1.00 37.16 ATOM 1789 CD1 LEU 1672 24.713 10.840 2.666 1.00 42.22 ATOM 1790 CD2 LEU 1672 26.863 9.665 2.237 1.00 33.93 ATOM 1791 C LEU 1672 24.078 10.280 −0.972 1.00 36.30 ATOM 1792 O LEU 1672 23.789 11.478 −0.949 1.00 39.09 ATOM 1793 N PHE 1673 24.770 9.723 −1.957 1.00 34.39 ATOM 1795 CA PHE 1673 25.266 10.504 −3.075 1.00 33.81 ATOM 1796 CB PHE 1673 26.553 9.874 −3.625 1.00 33.15 ATOM 1797 CG PHE 1673 27.661 9.761 −2.617 1.00 33.44 ATOM 1798 CD1 PHE 1673 28.323 8.545 −2.419 1.00 32.17 ATOM 1799 CD2 PHE 1673 28.055 10.867 −1.861 1.00 34.87 ATOM 1800 CE1 PHE 1673 29.346 8.419 −1.484 1.00 31.98 ATOM 1801 CE2 PHE 1673 29.090 10.757 −0.919 1.00 36.31 ATOM 1802 CZ PHE 1673 29.736 9.525 −0.732 1.00 34.55 ATOM 1803 C PHE 1673 24.273 10.670 −4.217 1.00 34.79 ATOM 1804 O PHE 1673 24.135 11.754 −4.765 1.00 35.74 ATOM 1805 N ASP 1674 23.584 9.588 −4.572 1.00 37.31 ATOM 1807 CA ASP 1674 22.650 9.601 −5.698 1.00 35.61 ATOM 1808 CE ASP 1674 22.917 8.392 −6.600 1.00 37.01 ATOM 1809 CG ASP 1674 24.362 8.288 −7.041 1.00 41.02 ATOM 1810 OD1 ASP 1674 25.030 9.340 −7.194 1.00 43.07 ATOM 1811 OD2 ASP 1674 24.828 7.145 −7.251 1.00 42.24 ATOM 1812 C ASP 1674 21.162 9.632 −5.360 1.00 37.06 ATOM 1813 O ASP 1674 20.315 9.506 −6.257 1.00 36.37 ATOM 1814 N ARG 1675 20.840 9.745 −4.077 1.00 37.78 ATOM 1816 CA ARG 1675 19.445 9.791 −3.650 1.00 39.41 ATOM 1817 CB ARG 1675 18.832 11.137 −4.039 1.00 44.39 ATOM 1818 CG ARG 1675 19.413 12.299 −3.269 1.00 54.30 ATOM 1819 CD ARG 1675 19.516 13.551 −4.127 1.00 63.84 ATOM 1820 NE ARG 1675 20.060 14.664 −3.349 1.00 73.69 ATOM 1822 CZ ARG 1675 19.652 15.925 −3.453 1.00 77.10 ATOM 1823 NH1 ARG 1675 18.695 16.253 −4.312 1.00 −79.65 ATOM 1826 NH2 ARG 1675 20.177 16.855 −2.665 1.00 79.31 ATOM 1829 C ARG 1675 18.617 8.639 −4.221 1.00 37.46 ATOM 1830 O ARG 1675 17.447 8.808 −4.557 1.00 38.57 ATOM 1831 N ILE 1676 19.235 7.475 −4.351 1.00 34.37 ATOM 1833 CA ILE 1676 18.545 6.313 −4.874 1.00 32.99 ATOM 1834 CB ILE 1676 19.358 5.644 −5.976 1.00 33.98 ATOM 1835 CG2 ILE 1676 18.552 4.529 −6.602 1.00 35.04 ATOM 1836 CG1 ILE 1676 19.708 6.663 −7.050 1.00 34.92 ATOM 1837 CD1 ILE 1676 20.799 6.200 −7.962 1.00 41.16 ATOM 1838 C ILE 1676 18.315 5.315 −3.743 1.00 31.55 ATOM 1839 O ILE 1676 19.245 4.632 −3.300 1.00 30.65 ATOM 1840 N TYR 1677 17.082 5.279 −3.246 1.00 30.88 ATOM 1842 CA TYR 1677 16.701 4.371 −2.173 1.00 27.10 ATOM 1843 CE TYR 1677 15.771 5.074 −1.208 1.00 28.30 ATOM 1844 CG TYR 1677 16.457 6.136 −0.406 1.00 30.61 ATOM 1845 CD1 TYR 1677 16.598 7.432 −0.905 1.00 30.82 ATOM 1846 CE1 TYR 1677 17.212 8.424 −0.159 1.00 30.75 ATOM 1847 CD2 TYR 1677 16.952 5.857 0.863 1.00 29.75 ATOM 1848 CE2 TYR 1677 17.567 6.842 1.621 1.00 32.62 ATOM 1849 CZ TYR 1677 17.688 8.125 1.110 1.00 34.51 ATOM 1850 OH TYR 1677 18.238 9.118 1.888 1.00 38.89 ATOM 1852 C TYR 1677 16.029 3.149 −2.743 1.00 25.47 ATOM 1853 O TYR 1677 15.132 3.264 −3.578 1.00 26.00 ATOM 1854 N THR 1678 16.459 1.983 −2.272 1.00 24.27 ATOM 1856 CA THR 1678 15.942 0.701 −2.734 1.00 24.09 ATOM 1857 CB THR 1678 16.830 0.123 −3.853 1.00 24.19 ATOM 1858 OG1 THR 1678 18.165 −0.008 −3.349 1.00 27.81 ATOM 1860 CG2 THR 1678 16.843 1.009 −5.085 1.00 24.15 ATOM 1861 C THR 1678 15.979 −0.297 −1.577 1.00 25.02 ATOM 1862 O THR 1678 16.379 0.036 −0.465 1.00 27.65 ATOM 1863 N HIS 1679 15.569 −1.530 −1.844 1.00 25.04 ATOM 1865 CA HIS 1679 15.591 −2.560 −0.818 1.00 24.35 ATOM 1866 CB HIS 1679 14.853 −3.812 −1.298 1.00 23.78 ATOM 1867 CG HIS 1679 13.390 −3.592 −1.536 1.00 27.24 ATOM 1868 CD2 HIS 1679 12.627 −3.758 −2.643 1.00 28.22 ATOM 1869 ND1 HIS 1679 12.532 −3.137 −0.551 1.00 30.64 ATOM 1871 CE1 HIS 1679 11.310 −3.028 −1.041 1.00 28.13 ATOM 1872 NE2 HIS 1679 11.339 −3.400 −2.307 1.00 28.52 ATOM 1874 C HIS 1679 17.056 −2.846 −0.514 1.00 22.52 ATOM 1875 O HIS 1679 17.419 −3.179 0.613 1.00 22.58 ATOM 1876 N GLN 1680 17.898 −2.604 −1.516 1.00 24.34 ATOM 1878 CA GLN 1680 19.341 −2.800 −1.406 1.00 23.52 ATOM 1879 CB GLN 1680 19.998 −2.781 −2.782 1.00 25.36 ATOM 1880 CG GLN 1680 19.741 −4.050 −3.577 1.00 33.28 ATOM 1881 CD GLN 1680 19.212 −3.763 −4.949 1.00 34.68 ATOM 1882 OE1 GLN 1680 18.683 −2.686 −5.187 1.00 41.24 ATOM 1883 NE2 GLN 1680 19.357 −4.713 −5.867 1.00 32.10 ATOM 1886 C GLN 1680 19.998 −1.767 −0.514 1.00 23.38 ATOM 1887 O GLN 1680 20.925 −2.094 0.224 1.00 25.12 ATOM 1888 N SER 1681 19.533 −0.521 −0.562 1.00 20.87 ATOM 1890 CA SER 1681 20.133 0.480 0.303 1.00 20.53 ATOM 1891 CE SER 1681 19.821 1.919 −0.151 1.00 19.58 ATOM 1892 OG SER 1681 18.445 2.126 −0.425 1.00 20.67 ATOM 1894 C SER 1681 19.696 0.189 1.741 1.00 22.22 ATOM 1895 O SER 1681 20.439 0.455 2.681 1.00 23.62 ATOM 1896 N ASP 1682 18.530 −0.436 1.900 1.00 22.44 ATOM 1898 CA ASP 1682 18.054 −0.816 3.231 1.00 22.70 ATOM 1899 CB ASP 1682 16.607 −1.293 3.180 1.00 24.24 ATOM 1900 CG ASP 1682 15.603 −0.165 3.352 1.00 28.23 ATOM 1901 OD1 ASP 1682 14.410 −0.425 3.108 1.00 28.14 ATOM 1902 OD2 ASP 1682 15.976 0.960 3.757 1.00 25.23 ATOM 1903 C ASP 1682 18.926 −1.941 3.777 1.00 23.92 ATOM 1904 O ASP 1682 19.121 −2.057 4.990 1.00 26.24 ATOM 1905 N VAL 1683 19.433 −2.788 2.884 1.00 23.67 ATOM 1907 CA VAL 1683 20.300 −3.888 3.302 1.00 22.42 ATOM 1908 CB VAL 1683 20.562 −4.881 2.141 1.00 23.70 ATOM 1909 CG1 VAL 1683 21.724 −5.802 2.459 1.00 19.73 ATOM 1910 CG2 VAL 1683 19.292 −5.713 1.889 1.00 19.85 ATOM 1911 C VAL 1683 21.584 −3.298 3.860 1.00 21.94 ATOM 1912 O VAL 1683 22.030 −3.688 4.938 1.00 22.69 ATOM 1913 N TRP 1684 22.141 −2.320 3.154 1.00 20.51 ATOM 1915 CA TRP 1684 23.349 −1.633 3.611 1.00 20.31 ATOM 1916 CB TRP 1684 23.659 −0.446 2680 1.00 19.01 ATOM 1917 CG TRP 1684 24.802 0.410 3.145 1.00 20.67 ATOM 1918 CD2 TRP 1684 26.114 0.468 2.587 1.00 22.26 ATOM 1919 CE2 TRP 1684 26.890 1.316 3.408 1.00 21.22 ATOM 1920 CE3 TRP 1684 26.718 −0.127 1.463 1.00 22.51 ATOM 1921 CD1 TRP 1684 24.825 1.229 4.248 1.00 19.91 ATOM 1922 NE1 TRP 1684 26.079 1.763 4.414 1.00 18.59 ATOM 1924 CZ2 TRP 1684 28.236 1.586 3.148 1.00 20.81 ATOM 1925 CZ3 TRP 1684 28.059 0.141 1.204 1.00 22.01 ATOM 1926 CR2 TRP 1684 28.806 0.992 2.047 1.00 23.34 ATOM 1927 C TRP 1684 23.131 −1.150 5.069 1.00 21.49 ATOM 1928 O TRP 1684 23.958 −1.412 5.954 1.00 23.34 ATOM 1929 N SER 1685 22.015 −0.463 5.308 1.00 21.84 ATOM 1931 CA SER 1685 21.652 0.042 6.634 1.00 20.02 ATOM 1932 CE SER 1685 20.310 0.773 6.559 1.00 19.12 ATOM 1933 OG SER 1685 20.335 1.791 5.578 1.00 21.62 ATOM 1935 C SER 1685 21.551 −1.111 7.648 1.00 22.64 ATOM 1936 O SER 1685 21.908 −0.946 8.829 1.00 22.09 ATOM 1937 N PHE 1686 21.043 −2.266 7.202 1.00 22.44 ATOM 1939 CA PHE 1686 20.939 −3.438 8.075 1.00 22.91 ATOM 1940 CB PHE 1686 20.196 −4.588 7.380 1.00 23.75 ATOM 1941 CG PHE 1686 20.027 −5.808 8.256 1.00 23.61 ATOM 1942 CD1 PHE 1686 19.220 −5.757 9.388 1.00 21.21 ATOM 1943 CD2 PHE 1686 20.731 −6.976 7.990 1.00 23.91 ATOM 1944 CE1 PHE 1686 19.118 −6.836 10.240 1.00 20.66 ATOM 1945 CE2 PHE 1686 20.636 −8.074 8.841 1.00 22.47 ATOM 1946 CZ PHE 1686 19.828 −7.999 9.972 1.00 23.35 ATOM 1947 C PHE 1686 22.339 −3.904 8.522 1.00 22.60 ATOM 1948 O PHE 1686 22.526 −4.382 9.646 1.00 22.83 ATOM 1949 N GLY 1687 23.312 −3.770 7.626 1.00 23.82 ATOM 1951 CA GLY 1687 24.682 −4.140 7.941 1.00 22.58 ATOM 1952 C GLY 1687 25.175 −3.262 9.071 1.00 21.49 ATOM 1953 O GLY 1687 25.832 −3.749 9.990 1.00 21.62 ATOM 1954 N VAL 1688 24.849 −1.968 9.008 1.00 21.15 ATOM 1956 CA VAL 1688 25.229 −1.008 10.052 1.00 20.56 ATOM 1957 CE VAL 1688 24.894 0.479 9.647 1.00 17.69 ATOM 1958 CG1 VAL 1688 25.408 1.456 10.690 1.00 15.11 ATOM 1959 CG2 VAL 1688 25.518 0.821 8.314 1.00 11.54 ATOM 1960 C VAL 1688 24.494 −1.398 11.346 1.00 22.60 ATOM 1961 O VAL 1688 25.083 −1.407 12.428 1.00 25.23 ATOM 1962 N LEU 1689 23.215 −1.755 11.229 1.00 26.09 ATOM 1964 CA LEU 1689 22.423 −2.175 12.387 1.00 25.16 ATOM 1965 CB LEU 1689 20.976 −2.455 11.965 1.00 25.91 ATOM 1966 CG LEU 1689 19.913 −2.560 13.068 1.00 27.54 ATOM 1967 CD1 LEU 1689 18.557 −2.241 12.496 1.00 28.11 ATOM 1968 CD2 LEU 1689 19.898 −3.940 13.704 1.00 31.67 ATOM 1969 C LEU 1689 23.055 −3.426 13.018 1.00 27.49 ATOM 1970 O LEU 1689 23.128 −3.532 14.246 1.00 28.99 ATOM 1971 N LEU 1690 23.485 −4.374 12.180 1.00 27.67 ATOM 1973 CA LEU 1690 24.149 −5.596 12.643 1.00 26.76 ATOM 1974 CE LEU 1690 24.616 −6.453 11.456 1.00 28.58 ATOM 1975 CG LEU 1690 23.651 −7.406 10.733 1.00 29.46 ATOM 1976 CD1 LEU 1690 24.372 −8.064 9.565 1.00 27.79 ATOM 1977 CD2 LEU 1690 23.130 −8.488 11.691 1.00 28.15 ATOM 1978 C LEU 1690 25.362 −5.176 13.476 1.00 26.19 ATOM 1979 O LEU 1690 25.565 −5.670 14.597 1.00 25.29 ATOM 1980 N TRP 1691 26.124 −4.217 12.946 1.00 25.89 ATOM 1982 CA TRP 1691 27.302 −3.682 13.631 1.00 27.31 ATOM 1983 CE TRP 1691 27.979 −2.628 12.755 1.00 25.21 ATOM 1984 CG TRP 1691 29.338 −2.170 13.257 1.00 27.00 ATOM 1985 CD2 TRP 1691 29.606 −1.060 14.134 1.00 24.28 ATOM 1986 CE2 TRP 1691 31.001 −0.988 14.297 1.00 23.03 ATOM 1987 CE3 TRP 1691 28.792 −0.118 14.778 1.00 22.80 ATOM 1988 CD1 TRP 1691 30.562 −2.712 12.944 1.00 24.10 ATOM 1989 NE1 TRP 1691 31.557 −2.010 13.567 1.00 23.41 ATOM 1991 CZ2 TRP 1691 31.617 −0.011 15.097 1.00 25.00 ATOM 1992 CZ3 TRP 1691 29.398 0.851 15.573 1.00 26.78 ATOM 1993 CH2 TRP 1691 30.802 0.900 15.719 1.00 27.78 ATOM 1994 C TRP 1691 26.947 −3.088 15.012 1.00 28.70 ATOM 1995 O TRP 1691 27.708 −3.245 15.974 1.00 29.56 ATOM 1996 N GLU 1692 25.808 −2.400 15.104 1.00 29.51 ATOM 1998 CA GLU 1692 25.349 −1.817 16.371 1.00 27.55 ATOM 1999 CE GLU 1692 24.120 −0.935 16.171 1.00 28.35 ATOM 2000 CG GLU 1692 24.273 0.221 15.219 1.00 24.70 ATOM 2001 CD GLU 1692 22.982 0.989 15.100 1.00 25.44 ATOM 2002 OE1 GLU 1692 22.224 0.744 14.148 1.00 24.34 ATOM 2003 OE2 GLU 1692 22.696 1.816 15.982 1.00 27.57 ATOM 2004 C GLU 1692 24.958 −2.918 17.352 1.00 28.74 ATOM 2005 O GLU 1692 25.099 −2.753 18.557 1.00 28.76 ATOM 2006 N ILE 1693 24.421 −4.023 16.844 1.00 29.23 ATOM 2008 CA ILE 1693 24.027 −5.125 17.712 1.00 27.48 ATOM 2009 CB ILE 1693 23.205 −6.226 16.944 1.00 28.80 ATOM 2010 CG2 ILE 1693 22.983 −7.469 17.842 1.00 22.98 ATOM 2011 CG1 ILE 1693 21.840 −5.658 16.508 1.00 27.36 ATOM 2012 CD1 ILE 1693 21.005 −6.585 15.635 1.00 24.84 ATOM 2013 C ILE 1693 25.259 −5.750 18.357 1.00 27.27 ATOM 2014 O ILE 1693 25.320 −5.902 19.575 1.00 28.15 ATOM 2015 N PHE 1694 26.273 −6.043 17.552 1.00 27.83 ATOM 2017 CA PHE 1694 27.473 −6.677 18.095 1.00 29.88 ATOM 2018 CB PHE 1694 28.143 −7.525 17.011 1.00 28.66 ATOM 2019 CG PHE 1694 27.223 −8.574 16.463 1.00 29.92 ATOM 2020 CD1 PHE 1694 26.628 −8.424 15.220 1.00 30.20 ATOM 2021 CD2 PHE 1694 26.809 −9.630 17.269 1.00 30.81 ATOM 2022 CE1 PHE 1694 25.625 −9.294 14.801 1.00 32.42 ATOM 2023 CE2 PHE 1694 25.805 −10.508 16.857 1.00 32.30 ATOM 2024 CZ PHE 1694 25.210 −10.337 15.628 1.00 31.13 ATOM 2025 C PHE 1694 28.429 −5.784 18.890 1.00 31.07 ATOM 2026 O PHE 1694 29.376 −6.273 19.509 1.00 33.16 ATOM 2027 N THR 1695 28.157 −4.480 18.897 1.00 29.20 ATOM 2029 CA THR 1695 28.934 −3.532 19.670 1.00 27.38 ATOM 2030 CB THR 1695 29.412 −2.333 18.823 1.00 24.77 ATOM 2031 OG1 THR 1695 28.287 −1.652 18.274 1.00 26.27 ATOM 2033 CG2 THR 1695 30.305 −2.800 17.706 1.00 20.18 ATOM 2034 C THR 1695 28.053 −3.034 20.822 1.00 29.84 ATOM 2035 O THR 1695 28.430 −2.103 21.548 1.00 32.77 ATOM 2036 N LEU 1696 26.898 −3.687 20.988 1.00 28.52 ATOM 2038 CA LEU 1696 25.915 −3.364 22.029 1.00 28.82 ATOM 2039 CB LEU 1696 26.356 −3.886 23.394 1.00 32.50 ATOM 2040 CG LEU 1696 26.658 −5.379 23.476 1.00 33.24 ATOM 2041 CD1 LEU 1696 27.205 −5.717 24.849 1.00 34.15 ATOM 2042 CD2 LEU 1696 25.398 −6.150 23.191 1.00 37.24 ATOM 2043 C LEU 1696 25.553 −1.888 22.131 1.00 26.98 ATOM 2044 O LEU 1696 25.579 −1.297 23.207 1.00 27.59 ATOM 2045 N GLY 1697 25.148 −1.317 21.007 1.00 27.86 ATOM 2047 CA GLY 1697 24.767 0.074 20.980 1.00 27.40 ATOM 2048 C GLY 1697 25.927 0.962 20.618 1.00 27.47 ATOM 2049 O GLY 1697 25.957 2.132 20.998 1.00 28.78 ATOM 2050 N GLY 1698 26.888 0.416 19.885 1.00 27.26 ATOM 2052 CA GLY 1698 28.031 1.212 19.482 1.00 29.54 ATOM 2053 C GLY 1698 27.651 2.301 18.492 1.00 31.17 ATOM 2054 O GLY 1698 26.669 2.177 17.755 1.00 33.73 ATOM 2055 N SER 1699 28.418 3.380 18.481 1.00 29.96 ATOM 2057 CA SER 1699 28.168 4.491 17.577 1.00 29.37 ATOM 2058 CB SER 1699 28.438 5.810 18.319 1.00 31.77 ATOM 2059 OG SER 1699 28.575 6.919 17.431 1.00 38.42 ATOM 2061 C SER 1699 29.093 4.350 16.369 1.00 27.98 ATOM 2062 O SER 1699 30.299 4.310 16.529 1.00 28.18 ATOM 2063 N PRO 1700 28.537 4.240 15.153 1.00 29.62 ATOM 2064 CD PRO 1700 27.104 4.259 14.794 1.00 31.22 ATOM 2065 CA PRO 1700 29.381 4.107 13.958 1.00 28.95 ATOM 2066 CB PRO 1700 28.356 4.003 12.807 1.00 27.21 ATOM 2067 CG PRO 1700 27.095 3.556 13.460 1.00 29.33 ATOM 2068 C PRO 1700 30.205 5.379 13.773 1.00 28.78 ATOM 2069 O PRO 1700 29.737 6.469 14.110 1.00 30.04 ATOM 2070 N TYR 1701 31.426 5.239 13.264 1.00 28.35 ATOM 2072 CA TYR 1701 32.296 6.390 12.987 1.00 30.77 ATOM 2073 CB TYR 1701 31.921 6.987 11.615 1.00 31.67 ATOM 2074 CG TYR 1701 32.060 6.037 10.454 1.00 34.61 ATOM 2075 CD1 TYR 1701 3.095 25.673 9.686 1.00 38.26 ATOM 2076 CE1 TYR 1701 31.083 4.806 8.587 1.00 40.99 ATOM 2077 CD2 TYR 1701 33.301 5.520 10.106 1.00 38.16 ATOM 2078 CE2 TYR 1701 33.449 4.662 9.020 1.00 41.04 ATOM 2079 CZ TYR 1701 32.343 4.312 8.263 1.00 43.11 ATOM 2080 OH TYR 1701 32.531 3.478 7.181 1.00 49.53 ATOM 2082 C TYR 1701 32.305 7.532 14.029 1.00 31.41 ATOM 2083 O TYR 1701 32.026 8.689 13.698 1.00 33.59 ATOM 2084 N PRO 1702 32.635 7.230 15.296 1.00 30.92 ATOM 2085 CD PRO 1702 32.998 5.938 15.888 1.00 32.30 ATOM 2086 CA PRO 1702 32.656 8.283 16.314 1.00 30.05 ATOM 2087 CB PRO 1702 33.123 7.548 17.561 1.00 27.77 ATOM 2088 CG PRO 1702 32.676 6.174 17.338 1.00 32.34 ATOM 2089 C PRO 1702 33.659 9.366 15.944 1.00 31.42 ATOM 2090 O PRO 1702 34.769 9.055 15.513 1.00 30.95 ATOM 2091 N GLY 1703 33.257 10.627 16.117 1.00 31.30 ATOM 2093 CA GLY 1703 34.122 11.751 15.817 1.00 29.66 ATOM 2094 C GLY 1703 34.172 12.138 14.351 1.00 31.00 ATOM 2095 O GLY 1703 34.752 13.165 13.999 1.00 30.69 ATOM 2096 N VAL 1704 33.551 11.331 13.491 1.00 31.11 ATOM 2098 CA VAL 1704 33.553 11.610 12.059 1.00 29.88 ATOM 2099 CB VAL 1704 33.539 10.310 11.244 1.00 28.41 ATOM 2100 CG1 VAL 1704 33.585 10.624 9.750 1.00 26.24 ATOM 2101 CG2 VAL 1704 34.702 9.429 11.649 1.00 24.10 ATOM 2102 C VAL 1704 32.396 12.508 11.604 1.00 30.80 ATOM 2103 O VAL 1704 31.224 12.146 11.712 1.00 32.50 ATOM 2104 N PRO 1705 32.718 13.705 11.104 1.00 30.86 ATOM 2105 CD PRO 1705 34.039 14.350 11.077 1.00 30.59 ATOM 2106 CA PRO 1705 31.682 14.625 10.645 1.00 31.47 ATOM 2107 CB PRO 1705 32.400 15.971 10.680 1.00 32.75 ATOM 2108 CG PRO 1705 33.774 15.607 10.289 1.00 32.59 ATOM 2109 C PRO 1705 31.258 14.264 9.239 1.00 32.19 ATOM 2110 O PRO 1705 31.974 13.536 8.549 1.00 33.91 ATOM 2111 N VAL 1706 30.124 14.814 8.806 1.00 32.57 ATOM 2113 CA VAL 1706 29.560 14.576 7.474 1.00 31.80 ATOM 2114 CB VAL 1706 28.483 15.632 7.172 1.00 34.66 ATOM 2115 CG1 VAL 1706 28.022 15.538 5.738 1.00 39.06 ATOM 2116 CG2 VAL 1706 27.309 15.455 8.106 1.00 36.62 ATOM 2117 C VAL 1706 30.578 14.560 6.320 1.00 31.58 ATOM 2118 O VAL 1706 30.682 −13.585 5.570 1.00 32.35 ATOM 2119 N GLU 1707 31.326 15.649 6.189 1.00 31.46 ATOM 2121 CA GLU 1707 32.329 15.788 5.139 1.00 31.68 ATOM 2122 CB GLU 1707 33.021 17.148 5.267 1.00 32.59 ATOM 2123 C GLU 1707 33.381 14.678 5.114 1.00 32.23 ATOM 2124 O GLU 1707 33.740 14.183 4.050 1.00 33.47 ATOM 2125 N GLU 1708 33.902 14.316 6.279 1.00 32.90 ATOM 2127 CA GLU 1708 34.909 13.268 6.352 1.00 33.86 ATOM 2128 CB GLU 1708 35.570 13.244 7.730 1.00 38.54 ATOM 2129 CG GLU 1708 36.190 14.575 8.165 1.00 47.63 ATOM 2130 CD GLU 1708 37.442 14.962 7.383 1.00 58.35 ATOM 2131 OE1 GLU 1708 38.117 14.067 6.816 1.00 62.88 ATOM 2132 OE2 GLU 1708 37.770 16.176 7.355 1.00 64.79 ATOM 2133 C GLU 1708 34.276 11.921 6.043 1.00 33.56 ATOM 2134 O GLU 1708 34.927 11.038 5.489 1.00 34.18 ATOM 2135 N LEU 1709 32.997 11.774 6.374 1.00 32.91 ATOM 2137 CA LEU 1709 32.285 10.532 6.108 1.00 33.83 ATOM 2138 CB LEU 1709 30.862 10.563 6.685 1.00 32.28 ATOM 2139 CG LEU 1709 30.015 9.363 6.231 1.00 32.92 ATOM 2140 CD1 LEU 1709 30.541 8.071 6.853 1.00 28.37 ATOM 2141 CD2 LEU 1709 28.563 9.580 6.568 1.00 31.90 ATOM 2142 C LEU 1709 32.222 10.283 4.606 1.00 34.15 ATOM 2143 O LEU 1709 32.412 9.152 4.156 1.00 34.75 ATOM 2144 N PHE 1710 31.918 11.332 3.844 1.00 33.83 ATOM 2146 CA PHE 1710 31.828 11.246 2.388 1.00 32.90 ATOM 2147 CB PHE 1710 31.531 12.622 1.787 1.00 34.85 ATOM 2148 CG PHE 1710 30.162 13.132 2.082 1.00 38.60 ATOM 2149 CD1 PHE 1710 29.150 12.268 2.469 1.00 43.69 ATOM 2150 CD2 PHE 1710 29.882 14.480 1.984 1.00 45.10 ATOM 2151 CE1 PHE 1710 27.873 12.742 2.764 1.00 46.23 ATOM 2152 CE2 PHE 1710 28.611 14.966 2.274 1.00 48.15 ATOM 2153 CZ PHE 1710 27.603 14.086 2.670 1.00 46.90 ATOM 2154 C PHE 1710 33.131 10.739 1.803 1.00 31.84 ATOM 2155 O PHE 1710 33.134 9.931 0.877 1.00 29.97 ATOM 2156 N LYS 1711 34.231 11.224 2.373 1.00 32.45 ATOM 2158 CA LYS 1711 35.582 10.860 1.947 1.00 34.53 ATOM 2159 CB LYS 1711 36.588 11.755 2.675 1.00 36.17 ATOM 2160 CG LYS 1711 38.008 11.669 2.182 1.00 41.07 ATOM 2161 CD LYS 1711 38.912 12.582 3.001 1.00 46.23 ATOM 2162 CE LYS 1711 40.311 12.648 2.418 1.00 51.79 ATOM 2163 NZ LYS 1711 41.036 11.360 2.556 1.00 57.27 ATOM 2167 C LYS 1711 35.867 9.375 2.215 1.00 33.82 ATOM 2168 O LYS 1711 36.451 8.688 1.376 1.00 33.20 ATOM 2169 N LEU 1712 35.439 8.885 3.382 1.00 34.52 ATOM 2171 CA LEU 1712 35.618 7.477 3.754 1.00 33.25 ATOM 2172 CE LEU 1712 35.094 7.211 5.189 1.00 30.99 ATOM 2173 CG LEU 1712 35.746 7.917 6.393 1.00 29.71 ATOM 2174 CD1 LEU 1712 35.047 7.552 7.678 1.00 24.11 ATOM 2175 CD2 LEU 1712 37.208 7.552 6.497 1.00 32.21 ATOM 2176 C LEU 1712 34.833 6.631 2.744 1.00 32.16 ATOM 2177 O LEU 1712 35.378 5.732 2.109 1.00 32.77 ATOM 2178 N LEU 1713 33.562 6.967 2.563 1.00 31.72 ATOM 2180 CA LEU 1713 32.700 6.259 1.637 1.00 33.60 ATOM 2181 CB LEU 1713 31.299 6.879 1.619 1.00 36.57 ATOM 2182 CG LEU 1713 30.522 6.711 2.930 1.00 37.60 ATOM 2183 CD1 LEU 1713 29.284 7.575 2.927 1.00 35.03 ATOM 2184 CD2 LEU 1713 30.182 5.246 3.157 1.00 33.22 ATOM 2185 C LEU 1713 33.285 6.248 0.236 1.00 35.33 ATOM 2186 O LEU 1713 33.318 5.203 −0.407 1.00 36.00 ATOM 2187 N LYS 1714 33.741 7.405 −0.234 1.00 36.24 ATOM 2189 CA LYS 1714 34.331 7.501 −1.566 1.00 36.35 ATOM 2190 CB LYS 1714 34.707 8.946 −1.900 1.00 35.82 ATOM 2191 CG LYS 1714 33.520 9.837 −2.168 1.00 37.23 ATOM 2192 CD LYS 1714 32.712 9.324 −3.337 1.00 40.53 ATOM 2193 CE LYS 1714 31.506 10.198 −3.600 1.00 44.51 ATOM 2194 NZ LYS 1714 30.747 9.724 −4.804 1.00 50.76 ATOM 2198 C LYS 1714 35.559 6.613 −1.701 1.00 37.60 ATOM 2199 O LYS 1714 35.808 6.039 −2.764 1.00 40.82 ATOM 2200 N GLU 1715 36.299 6.452 −0.615 1.00 35.61 ATOM 2202 CA GLU 1715 37.496 5.630 −0.658 1.00 34.65 ATOM 2203 CB GLU 1715 38.517 6.188 0.320 1.00 37.83 ATOM 2204 CG GLU 1715 38.897 7.613 −0.036 1.00 42.28 ATOM 2205 CD GLU 1715 39.634 8.342 1.061 1.00 45.64 ATOM 2206 OE1 GLU 1715 39.928 7.726 2.114 1.00 43.09 ATOM 2207 OE2 GLU 1715 39.918 9.544 0.853 1.00 47.56 ATOM 2208 C GLU 1715 37.244 4.145 −0.419 1.00 32.94 ATOM 2209 O GLU 1715 38.177 3.348 −0.419 1.00 33.31 ATOM 2210 N GLY 1716 35.983 3.779 −0.213 1.00 29.12 ATOM 2212 CA GLY 1716 35.634 2.391 0.004 1.00 26.02 ATOM 2213 C GLY 1716 35.946 1.895 1.396 1.00 29.60 ATOM 2214 O GLY 1716 36.223 0.715 1.588 1.00 29.81 ATOM 2215 N HIS 1717 35.879 2.783 2.379 1.00 29.97 ATOM 2217 CA HIS 1717 36.158 2.409 3.763 1.00 30.78 ATOM 2218 CE HIS 1717 36.369 3.659 4.623 1.00 33.25 ATOM 2219 CG HIS 1717 36.653 3.360 6.067 1.00 34.70 ATOM 2220 CD2 HIS 1717 37.820 3.155 6.715 1.00 32.77 ATOM 2221 ND1 HIS 1717 35.656 3.219 7.010 1.00 36.90 ATOM 2223 CE1 HIS 1717 36.200 2.932 8.180 1.00 35.87 ATOM 2224 NE2 HIS 1717 37.513 2.887 8.027 1.00 31.93 ATOM 2226 C HIS 1717 35.035 1.577 4.375 1.00 29.63 ATOM 2227 O HIS 1717 33.861 1.847 4.133 1.00 30.82 ATOM 2228 N ARG 1718 35.406 0.600 5.201 1.00 27.92 ATOM 2230 CA ARG 1718 34.436 −0.258 5.878 1.00 27.30 ATOM 2231 CB ARG 1718 34.379 −1.641 5.236 1.00 24.10 ATOM 2232 CG ARG 1718 33.939 −1.655 3.789 1.00 26.52 ATOM 2233 CD ARG 1718 32.469 −1.288 3.627 1.00 26.96 ATOM 2234 NE ARG 1718 32.020 −1.374 2.232 1.00 24.41 ATOM 2236 CZ ARG 1718 32.090 −0.377 1.352 1.00 25.51 ATOM 2237 NH1 ARG 1718 32.611 0.801 1.706 1.00 23.61 ATOM 2240 NH2 ARG 1718 31.553 −0.521 0.149 1.00 21.28 ATOM 2243 C ARG 1718 34.881 −0.384 7.330 1.00 28.81 ATOM 2244 O ARG 1718 36.080 −0.425 7.611 1.00 29.77 ATOM 2245 N MET 1719 . 33.920 −0.377 8.250 1.00 30.40 ATOM 2247 CA MET 1719 34.215 −0.485 9.673 1.00 30.62 ATOM 2248 CB MET 1719 32.942 −0.339 10.497 1.00 28.91 ATOM 2249 CG MET 1719 32.235 1.003 10.316 1.00 30.85 ATOM 2250 SD MET 1719 30.829 1.237 11.432 1.00 33.27 ATOM 2251 CE MET 1719 29.521 0.416 10.561 1.00 31.81 ATOM 2252 C MET 1719 34.900 −1.793 10.005 1.00 31.32 ATOM 2253 O MET 1719 34.755 −2.769 9.278 1.00 31.47 ATOM 2254 N ASP 1720 35.651 −1.799 11.103 1.00 33.78 ATOM 2256 CA ASP 1720 36.387 −2.983 11.550 1.00 33.45 ATOM 2257 CB ASP 1720 37.478 −2.580 12.546 1.00 36.99 ATOM 2258 CG ASP 1720 38.585 −1.762 11.908 1.00 41.56 ATOM 2259 OD1 ASP 1720 38.403 −1.339 10.742 1.00 48.43 ATOM 2260 OD2 ASP 1720 39.634 −1.546 12.568 1.00 40.99 ATOM 2261 C ASP 1720 35.473 −4.001 12.211 1.00 32.12 ATOM 2262 O ASP 1720 34.381 −3.657 12.668 1.00 30.89 ATOM 2263 N LYS 1721 35.944 −5.241 12.328 1.00 31.82 ATOM 2265 CA LYS 1721 35.127 −6.270 12.953 1.00 31.71 ATOM 2266 CB LYS 1721 35.691 −7.679 12.747 1.00 32.34 ATOM 2267 CG LYS 1721 34.762 −8.738 13.344 1.00 34.85 ATOM 2268 CD LYS 1721 35.111 −10.155 12.961 1.00 37.39 ATOM 2269 CE LYS 1721 36.266 −10.674 13.765 1.00 41.42 ATOM 2270 NZ LYS 1721 36.348 −12.154 13.635 1.00 46.55 ATOM 2274 C LYS 1721 35.007 −6.018 14.430 1.00 33.40 ATOM 2275 O LYS 1721 36.017 −5.879 15.121 1.00 34.26 ATOM 2276 N PRO 1722 33.768 −5.924 14.934 1.00 34.26 ATOM 2277 CD PRO 1722 32.494 −6.002 14.203 1.00 32.16 ATOM 2278 CA PRO 1722 33.546 −5.692 16.362 1.00 35.84 ATOM 2279 CB PRO 1722 32.027 −5.682 16.473 1.00 35.35 ATOM 2280 CG PRO 1722 31.575 −5.255 15.108 1.00 35.35 ATOM 2281 C PRO 1722 34.105 −6.904 17.099 1.00 40.41 ATOM 2282 O PRO 1722 34.010 −8.038 16.607 1.00 41.14 ATOM 2283 N SER 1723 34.739 −6.680 18.240 1.00 43.60 ATOM 2285 CA SER 1723 35.260 −7.808 18.999 1.00 45.51 ATOM 2286 CB SER 1723 36.078 −7.324 20.191 1.00 45.30 ATOM 2287 OG SER 1723 35.384 −6.300 20.879 1.00 49.62 ATOM 2289 C SER 1723 34.031 −8.589 19.460 1.00 46.39 ATOM 2290 O SER 1723 32.939 −8.028 19.614 1.00 45.16 ATOM 2291 N ASN 1724 34.199 −9.891 19.631 1.00 48.53 ATOM 2293 CA ASN 1724 33.088 −10.723 20.065 1.00 51.13 ATOM 2294 CB ASN 1724 32.509 −10.194 21.390 1.00 56.87 ATOM 2295 CG ASN 1724 33.595 −9.892 22.427 1.00 61.65 ATOM 2296 OD1 ASN 1724 34.503 −10.702 22.649 1.00 63.73 ATOM 2297 ND2 ASN 1724 33.526 −8.713 23.039 1.00 64.64 ATOM 2300 C ASN 1724 32.034 −10.743 18.941 1.00 48.83 ATOM 2301 O ASN 1724 30.846 −10.534 19.145 1.00 50.50 ATOM 2302 N CYS 1725 32.511 −10.977 17.734 1.00 45.23 ATOM 2304 CA CYS 1725 31.654 −11.056 16.570 1.00 42.33 ATOM 2305 CB CYS 1725 31.570 −9.702 15.854 1.00 41.48 ATOM 2306 SG CYS 1725 30.711 −9.751 14.275 1.00 40.38 ATOM 2307 C CYS 1725 32.383 −12.077 15.725 1.00 39.64 ATOM 2308 O CYS 1725 33.601 −12.004 15.579 1.00 42.00 ATOM 2309 N THR 1726 31.664 −13.090 15.263 1.00 35.96 ATOM 2311 CA THR 1726 32.275 −14.139 14.459 1.00 33.61 ATOM 2312 CB THR 1726 31.301 −15.326 14.326 1.00 33.29 ATOM 2313 OG1 THR 1.726 30.071 −14.904 13.711 1.00 34.53 ATOM 2315 CG2 THR 1726 30.981 −15.861 15.696 1.00 25.84 ATOM 2316 C THR 1726 32.720 −13.629 13.092 1.00 32.27 ATOM 2317 O THR 1726 32.257 −12.593 12.643 1.00 33.04 ATOM 2318 N ASN 1727 33.643 −14.315 12.434 1.00 32.98 ATOM 2320 CA ASN 1727 34.050 −13.850 11.114 1.00 34.97 ATOM 2321 CB ASN 1727 35.198 −14.680 10.541 1.00 39.89 ATOM 2322 CG ASN 1727 36.540 −14.271 11.103 1.00 45.37 ATOM 2323 OD1 ASN 1727 37.044 −13.177 10.826 1.00 48.43 ATOM 2324 ND2 ASN 1727 37.125 −15.141 11.909 1.00 45.88 ATOM 2327 C ASN 1727 32.846 −13.947 10.192 1.00 33.97 ATOM 2328 O ASN 1727 32.646 −13.088 9.341 1.00 35.07 ATOM 2329 N GLU 1728 32.024 −14.973 10.414 1.00 31.69 ATOM 2331 CA GLU 1728 30.814 −15.210 9.620 1.00 30.27 ATOM 2332 CB GLU 1728 30.141 −16.493 10.083 1.00 32.53 ATOM 2333 CG GLU 1728 28.932 −16.878 9.273 1.00 32.81 ATOM 2334 CD GLU 1728 28.353 −18.190 9.711 1.00 36.43 ATOM 2335 OE1 GLU 1728 28.339 −18.466 10.932 1.00 36.75 ATOM 2336 OE2 GLU 1728 27.908 −18.945 8.829 1.00 41.92 ATOM 2337 C GLU 1728 29.814 −14.049 9.681 1.00 28.70 ATOM 2338 O GLU 1728 29.234 −13.655 8.660 1.00 28.51 ATOM 2339 N LEU 1729 29.594 −13.517 10.880 1.00 26.77 ATOM 2341 CA LEU 1729 28.687 −12.393 11.040 1.00 26.80 ATOM 2342 CB LEU 1729 28.228 −12.274 12.490 1.00 27.91 ATOM 2343 CG LEU 1729 27.233 −13.355 12.913 1.00 30.71 ATOM 2344 CD1 LEU 1729 27.095 −13.345 14.428 1.00 35.79 ATOM 2345 CD2 LEU 1729 25.885 −13.141 12.253 1.00 25.70 ATOM 2346 C LEU 1729 29.319 −11.089 10.540 1.00 27.06 ATOM 2347 O LEU 1729 28.610 −10.177 10.126 1.00 30.27 ATOM 2348 N TYR 1730 30.650 −11.004 10.549 1.00 27.03 ATOM 2350 CA TYR 1730 31.328 −9.812 10.039 1.00 26.21 ATOM 2351 CB TYR 1730 32.792 −9.778 10.474 1.00 25.31 ATOM 2352 CG TYR 1730 33.538 −8.553 9.982 1.00 24.89 ATOM 2353 CD1 TYR 1730 33.012 −7.270 10.169 1.00 23.59 ATOM 2354 CE1 TYR 1730 33.655 −6.148 9.665 1.00 24.74 ATOM 2355 CD2 TYR 1730 34.739 −8.675 9.285 1.00 22.11 ATOM 2356 CE2 TYR 1730 35.399 −7.560 8.775 1.00 22.32 ATOM 2357 CZ TYR 1730 34.853 −6.295 8.962 1.00 26.07 ATOM 2358 OH TYR 1730 35.484 −5.181 8.418 1.00 22.70 ATOM 2360 C TYR 1730 31.227 −9.878 8.509 1.00 27.71 ATOM 2361 O TYR 1730 30.960 −8.875 7.843 1.00 28.05 ATOM 2362 N MET 1731 31.409 −11.081 7.977 1.00 27.92 ATOM 2364 CA MET 1731 31.306 −11.355 6.548 1.00 28.89 ATOM 2365 CB MET 1731 31.506 −12.853 6.317 1.00 35.84 ATOM 2366 CG MET 1731 31.068 −13.379 4.975 1.00 45.50 ATOM 2367 SD MET 1731 31.347 −15.167 4.865 1.00 56.40 ATOM 2368 CE MET 1731 32.106 −15.263 3.217 1.00 56.88 ATOM 2369 C MET 1731 29.916 −10.928 6.102 1.00 27.79 ATOM 2370 O MET 1731 29.755 −10.345 5.041 1.00 30.68 ATOM 2371 N MET 1732 28.915 −11.203 6.932 1.00 28.02 ATOM 2373 CA MET 1732 27.546 −10.804 6.639 1.00 25.74 ATOM 2374 CB MET 1732 26.598 −11.317 7.718 1.00 24.94 ATOM 2375 CG MET 1732 25.153 −10.911 7.492 1.00 22.96 ATOM 2376 SD MET 1732 24.008 −11.593 8.684 1.00 24.39 ATOM 2377 CE MET 1732 23.798 −13.272 8.002 1.00 18.04 ATOM 2378 C MET 1732 27.470 −9.273 6.559 1.00 25.81 ATOM 2379 O MET 1732 26.889 −8.729 5.620 1.00 26.85 ATOM 2380 N MET 1733 28.068 −8.587 7.537 1.00 24.84 ATOM 2382 CA MET 1733 28.092 −7.124 7.545 1.00 25.27 ATOM 2383 CB MET 1733 28.931 −6.600 8.700 1.00 25.97 ATOM 2384 CG MET 1733 28.342 −6.769 10.058 1.00 28.69 ATOM 2385 SD MET 1733 29.456 −6.094 11.295 1.00 29.06 ATOM 2386 CE MET 1733 28.927 −7.051 12.693 1.00 28.07 ATOM 2387 C MET 17.33 28.741 −6.628 6.270 1.00 26.97 ATOM 2388 O MET 1733 28.192 −5.771 5.581 1.00 28.37 ATOM 2389 N ARG 1734 29.922 −7.160 5.966 1.00 28.77 ATOM 2391 CA ARG 1734 30.664 −6.775 4.762 1.00 29.66 ATOM 2392 CB ARG 1734 32.027 −7.482 4.716 1.00 29.05 ATOM 2393 CG ARG 1734 32.968 −7.109 5.866 1.00 25.00 ATOM 2394 CD ARG 1734 33.247 −5.621 5.882 1.00 29.27 ATOM 2395 NE ARG 1734 33.911 −5.210 4.647 1.00 35.43 ATOM 2397 CZ ARG 1734 35.233 −5.220 4.466 1.00 38.24 ATOM 2398 NH1 ARG 1734 36.054 −5.601 5.445 1.00 36.47 ATOM 2401 NH2 ARG 1734 35.732 −4.907 3.277 1.00 38.57 ATOM 2404 C ARG 1734 29.859 −7.034 3.478 1.00 29.57 ATOM 2405 O ARG 1734 29.920 −6.242 2.538 1.00 29.55 ATOM 2406 N ASP 1735 29.095 −8.124 3.448 1.00 28.07 ATOM 2408 CA ASP 1735 28.259 −8.423 2.287 1.00 27.96 ATOM 2409 CB ASP 1735 27.634 −9.813 2.408 1.00 28.60 ATOM 2410 CG ASP 1735 28.664 −10.926 2.283 1.00 31.34 ATOM 2411 OD1 ASP 1735 29.785 −10.660 1.798 1.00 31.12 ATOM 2412 OD2 ASP 1735 28.356 −12.068 2.687 1.00 36.07 ATOM 2413 C ASP 1735 27.159 −7.368 2.155 1.00 27.24 ATOM 2414 O ASP 1735 26.846 −6.932 1.050 1.00 25.79 ATOM 2415 N CYS 1736 26.590 −6.951 3.288 1.00 26.53 ATOM 2417 CA CYS 1736 25.547 −5.930 3.314 1.00 24.35 ATOM 2418 CB CYS 1736 24.968 −5.765 4.731 1.00 22.01 ATOM 2419 SG CYS 1736 23.885 −7.101 5.281 1.00 21.52 ATOM 2420 C CYS 1736 26.119 −4.595 2.847 1.00 24.26 ATOM 2421 O CYS 1736 25.386 −3.725 2.368 1.00 24.19 ATOM 2422 N TRP 1737 27.432 −4.437 3.002 1.00 22.94 ATOM 2424 CA TRP 1737 28.104 −3.210 2.605 1.00 21.91 ATOM 2425 CB TRP 1737 29.146 −2.820 3.640 1.00 19.26 ATOM 2426 CG TRP 1737 28.572 −2.493 4.947 1.00 20.89 ATOM 2427 CD2 TRP 1737 29.226 −2.602 6.212 1.00 23.33 ATOM 2428 CE2 TRP 1737 28.315 −2.159 7.196 1.00 21.59 ATOM 2429 CE3 TRP 1737 30.506 −3.026 6.614 1.00 25.00 ATOM 2430 CD1 TRP 1737 27.319 −2.012 5.201 1.00 19.90 ATOM 2431 NE1 TRP 1737 27.158 −1.807 6.551 1.00 20.77 ATOM 2433 CZ2 TRP 1737 28.641 −2.127 8.563 1.00 19.89 ATOM 2434 CZ3 TRP 1737 30.825 −2.993 7.971 1.00 21.23 ATOM 2435 CH2 TRP 1737 29.896 −2.543 8.927 1.00 21.09 ATOM 2436 C TRP 1737 28.758 −3.266 1.232 1.00 23.54 ATOM 2437 O TRP 1737 29.653 −2.477 0.939 1.00 24.68 ATOM 2438 N HIS 1738 28.315 −4.185 0.382 1.00 24.37 ATOM 2440 CA HIS 1738 28.877 −4.287 −0.947 1.00 24.42 ATOM 2441 CB HIS 1738 28.243 −5.436 −1.728 1.00 23.72 ATOM 2442 CG HIS 1738 29.131 −5.985 −2.801 1.00 27.20 ATOM 2443 CD2 HIS 1738 29.595 −5.425 −3.948 1.00 26.45 ATOM 2444 ND1 HIS 1738 29.681 −7.255 −2.751 1.00 29.26 ATOM 2446 CE1 HIS 1738 30.436 −7.441 −3.816 1.00 29.25 ATOM 2447 NE2 HIS 1738 30.409 −6.358 −4.556 1.00 27.32 ATOM 2449 C HIS 1738 28.716 −2.970 −1.713 1.00 25.82 ATOM 2450 O HIS 1738 27.675 −2.314 −1.660 1.00 23.96 ATOM 2451 N ALA 1739 29.802 −2.564 −2.362 1.00 26.27 ATOM 2453 CA ALA 1739 29.825 −1.346 −3.158 1.00 25.46 ATOM 2454 CB ALA 1739 31.186 −1.180 −3.789 1.00 25.70 ATOM 2455 C ALA 1739 28.754 −1.443 −4.233 1.00 26.18 ATOM 2456 O ALA 1739 28.116 −0.455 −4.574 1.00 29.14 ATOM 2457 N VAL 1740 28.570 −2.643 −4.774 1.00 25.71 ATOM 2459 CA VAL 1740 27.560 −2.875 −5.802 1.00 26.12 ATOM 2460 CB VAL 1740 28.063 −3.841 −6.903 1.00 25.99 ATOM 2461 CG1 VAL 1740 27.102 −3.832 −8.090 1.00 23.37 ATOM 2462 CG2 VAL 1740 29.450 −3.440 −7.349 1.00 22.07 ATOM 2463 C VAL 1740 26.247 −3.400 −5.191 1.00 25.43 ATOM 2464 O VAL 1740 26.186 −4.550 −4.704 1.00 24.93 ATOM 2465 N PRO 1741 25.170 −2.585 −5.265 1.00 24.20 ATOM 2466 CD PRO 1741 25.151 −1.277 −5.953 1.00 18.88 ATOM 2467 CA PRO 1741 23.838 −2.914 −4.734 1.00 25.28 ATOM 2468 CB PRO 1741 22.953 −1.788 −5.294 1.00 22.75 ATOM 2469 CG PRO 1741 23.903 −0.632 −5.398 1.00 20.99 ATOM 2470 C PRO 1741 23.299 −4.296 −5.128 1.00 25.84 ATOM 2471 O PRO 1741 22.787 −5.036 −4.280 1.00 25.99 ATOM 2472 N SER 1742 23.425 −4.642 −6.407 1.00 26.48 ATOM 2474 CA SER 1742 22.942 −5.919 −6.930 1.00 25.19 ATOM 2475 CB SER 1742 23.151 −5.992 −8.440 1.00 25.68 ATOM 2476 OG SER 1742 24.530 −5.943 −8.769 1.00 27.46 ATOM 2478 C SER 1742 23.644 −7.100 −6.289 1.00 25.24 ATOM 2479 O SER 1742 23.124 −8.218 −6.300 1.00 26.09 ATOM 2480 N GLN 1743 24.826 −6.851 −5.731 1.00 23.88 ATOM 2482 CA GLN 1743 25.590 −7.917 −5.118 1.00 24.44 ATOM 2483 CB GLN 1743 27.069 −7.733 −5.437 1.00 27.26 ATOM 2484 CG GLN 1743 27.344 −7.784 −6.940 1.00 27.39 ATOM 2485 CD GLN 1743 26.803 −9.047 −7.581 1.00 26.46 ATOM 2486 OE1 GLN 1743 27.325 −10.136 −7.339 1.00 25.80 ATOM 2487 NE2 GLN 1743 25.760 −8.914 −8.393 1.00 27.42 ATOM 2490 C GLN 1743 25.348 −8.151 −3.633 1.00 23.20 ATOM 2491 O GLN 1743 25.810 −9.147 −3.083 1.00 22.90 ATOM 2492 N ARG 1744 24.628 −7.243 −2.984 1.00 22.15 ATOM 2494 CA ARG 1744 24.318 −7.398 −1.568 1.00 21.23 ATOM 2495 CB ARG 1744 23.767 −6.088 −0.998 1.00 19.01 ATOM 2496 CG ARG 1744 24.705 −4.916 −1.145 1.00 17.27 ATOM 2497 CD ARG 1744 24.091 −3.605 −0.679 1.00 14.79 ATOM 2498 NE ARG 1744 24.914 −2.493 −1.157 1.00 19.72 ATOM 2500 CZ ARG 1744 24.482 −1.258 −1.391 1.00 19.23 ATOM 2501 NH1 ARG 1744 23.201 −0.931 −1.201 1.00 15.90 ATOM 2504 NH2 ARG 1744 25.343 −0.343 −1.821 1.00 19.43 ATOM 2507 C ARG 1744 23.259 −8.496 −1.438 1.00 21.95 ATOM 2508 O ARG 1744 22.585 −8.827 −2.415 1.00 25.34 ATOM 2509 N PRO 1745 23.213 −9.184 −0.292 1.00 20.82 ATOM 2510 CD PRO 1745 24.191 −9.219 0.804 1.00 21.25 ATOM 2511 CA PRO 1745 22.204 −10.229 −0.127 1.00 21.39 ATOM 2512 CB PRO 1745 22.687 −10.980 1.117 1.00 21.69 ATOM 2513 CG PRO 1745 23.418 −9.916 1.886 1.00 22.62 ATOM 2514 C PRO 1745 20.833 −9.585 0.102 1.00 22.15 ATOM 2515 O PRO 1745 20.739 −8.402 0.426 1.00 23.29 ATOM 2516 N THR 1746 19.771 −10.349 −0.109 1.00 20.93 ATOM 2518 CA THR 1746 18.440 −9.827 0.107 1.00 19.90 ATOM 2519 CB THR 1746 17.391 −10.554 −0.783 1.00 20.21 ATOM 2520 OG1 THR 1746 17.484 −11.974 −0.584 1.00 22.03 ATOM 2522 CG2 THR 1746 17.609 −10.242 −2.255 1.00 20.82 ATOM 2523 C THR 1746 18.112 −10.095 1.557 1.00 19.77 ATOM 2524 O THR 1746 18.842 −10.823 2.228 1.00 19.19 ATOM 2525 N PHE 1747 17.010 −9.526 2.045 1.00 23.46 ATOM 2527 CA PHE 1747 16.582 −9.770 3.422 1.00 21.64 ATOM 2528 CB PHE 1747 15.473 −8.794 3.827 1.00 18.89 ATOM 2529 CG PHE 1747 15.987 −7.445 4.262 1.00 17.45 ATOM 2530 CD1 PHE 1747 16.757 −7.317 5.417 1.00 17.65 ATOM 2531 CD2 PHE 1747 15.712 −6.303 3.516 1.00 15.37 ATOM 2532 CE1 PHE 1747 17.242 −6.073 5.819 1.00 16.17 ATOM 2533 CE2 PHE 1747 16.189 −5.056 3.907 1.00 14.53 ATOM 2534 CZ PHE 1747 16.959 −4.941 5.065 1.00 16.88 ATOM 2535 C PHE 1747 16.118 −11.227 3.522 1.00 23.18 ATOM 2536 O PHE 1747 16.271 −11.873 4.548 1.00 24.04 ATOM 2537 N LYS 1748 15.570 −11.745 2.432 1.00 24.13 ATOM 2539 CA LYS 1748 15.137 −13.132 2.385 1.00 26.35 ATOM 2540 CB LYS 1748 14.502 −13.424 1.024 1.00 27.52 ATOM 2541 CG LYS 1748 14.034 −14.849 0.836 1.00 33.88 ATOM 2542 CD LYS 1748 13.598 −15.062 −0.600 1.00 41.83 ATOM 2543 CE LYS 1748 13.190 −16.506 −0.881 1.00 50.05 ATOM 2544 NZ LYS 1748 12.084 −16.986 0.005 1.00 55.70 ATOM 2548 C LYS 1748 16.359 −14.037 2.636 1.00 27.50 ATOM 2549 O LYS 1748 16.303 −14.950 3.459 1.00 31.18 ATOM 2550 N GLN 1749 17.467 −13.761 1.949 1.00 27.24 ATOM 2552 CA GLN 1749 18.699 −14.529 2.122 1.00 27.03 ATOM 2553 CB GLN 1749 19.797 −14.039 1.169 1.00 31.80 ATOM 2554 CG GLN 1749 19.501 −14.196 −0.323 1.00 38.57 ATOM 2555 CD GLN 1749 20.460 −13.385 −1.209 1.00 39.93 ATOM 2556 OE1 GLN 1749 20.025 −12.535 −1.974 1.00 39.90 ATOM 2557 NE2 GLN 1749 21.768 −13.620 −1.068 1.00 40.23 ATOM 2560 C GLN 1749 19.205 −14.380 3.552 1.00 25.98 ATOM 2561 O GLN 1749 19.533 −15.371 4.198 1.00 27.18 ATOM 2562 N LEU 1750 19.293 −13.133 4.018 1.00 25.20 ATOM 2564 CA LEU 1750 19.774 −12.823 5.369 1.00 25.74 ATOM 2565 CB LEU 1750 19.722 −11.317 5.631 1.00 20.99 ATOM 2566 CG LEU 1750 20.708 −10.468 4.831 1.00 20.90 ATOM 2567 CD1 LEU 1750 20.302 −8.987 4.822 1.00 19.88 ATOM 2568 CD2 LEU 1750 22.071 −10.643 5.426 1.00 17.26 ATOM 2569 C LEU 1750 18.985 −13.555 6.441 1.00 27.10 ATOM 2570 O LEU 1750 19.553 −14.094 7.392 1.00 27.89 ATOM 2571 N VAL 1751 17.672 −13.598 6.265 1.00 29.40 ATOM 2573 CA VAL 1751 16.798 −14.262 7.210 1.00 26.80 ATOM 2574 CB VAL 1751 15.324 −14.030 6.843 1.00 26.94 ATOM 2575 CG1 VAL 1751 14.429 −14.941 7.657 1.00 29.93 ATOM 2576 CG2 VAL 1751 14.941 −12.575 7.117 1.00 24.10 ATOM 2577 C VAL 1751 17.136 −15.745 7.228 1.00 27.80 ATOM 2578 O VAL 1751 17.223 −16.359 8.285 1.00 26.77 ATOM 2579 N GLU 1752 17.408 −16.300 6.056 1.00 32.26 ATOM 2581 CA GLU 1752 17.749 −17.717 5.966 1.00 35.72 ATOM 2582 CB GLU 1752 17.721 −18.173 4.504 1.00 39.33 ATOM 2583 CG GLU 1752 16.306 −18.078 3.911 1.00 49.41 ATOM 2584 CD GLU 1752 16.209 −18.421 2.429 1.00 55.88 ATOM 2585 OE1 GLU 1752 15.141 −18.138 1.835 1.00 58.00 ATOM 2586 OE2 GLU 1752 17.180 −18.978 1.863 1.00 61.03 ATOM 2587 C GLU 1752 19.093 −18.002 6.635 1.00 34.59 ATOM 2588 O GLU 1752 19.230 −18.975 7.393 1.00 33.95 ATOM 2589 N ASP 1753 20.057 −17.114 6.401 1.00 34.38 ATOM 2591 CA ASP 1753 21.393 −17.235 6.977 1.00 32.81 ATOM 2592 CB ASP 1753 22.338 −16.227 6.334 1.00 31.57 ATOM 2593 CG ASP 1753 22.628 −16.556 4.888 1.00 33.68 ATOM 2594 OD1 ASP 1753 22.573 −17.755 4.536 1.00 35.14 ATOM 2595 OD2 ASP 1753 22.914 −15.624 4.104 1.00 34.44 ATOM 2596 C ASP 1753 21.378 −17.058 8.489 1.00 32.04 ATOM 2597 O ASP 1753 21.997 −17.837 9.214 1.00 31.21 ATOM 2598 N LEU 1754 20.648 −16.045 8.955 1.00 31.00 ATOM 2600 CA LEU 1754 20.528 −15.754 10.382 1.00 29.46 ATOM 2601 CS LEU 1754 19.822 −14.426 10.598 1.00 23.47 ATOM 2602 CG LEU 1754 20.816 −13.309 10.318 1.00 23.58 ATOM 2603 CD1 LEU 1754 20.114 −11.963 10.128 1.00 20.46 ATOM 2604 CD2 LEU 1754 21.828 −13.282 11.462 1.00 19.18 ATOM 2605 C LEU 1754 19.806 −16.866 11.110 1.00 31.84 ATOM 2606 O LEU 1754 20.125 −17.178 12.254 1.00 30.78 ATOM 2607 N ASP 1755 18.832 −17.471 10.445 1.00 34.03 ATOM 2609 CA ASP 1755 18.116 −18.578 11.044 1.00 35.22 ATOM 2610 CS ASP 1755 16.973 −19.027 10.148 1.00 38.40 ATOM 2611 CG ASP 1755 16.159 −20.119 10.779 1.00 41.85 ATOM 2612 OD1 ASP 1755 15.560 −19.866 11.841 1.00 47.90 ATOM 2613 OD2 ASP 1755 16.142 −21.241 10.238 1.00 46.67 ATOM 2614 C ASP 1755 19.114 −19.724 11.222 1.00 36.79 ATOM 2615 O ASP 1755 19.114 −20.411 12.250 1.00 38.33 ATOM 2616 N ARG 1756 19.973 −19.920 10.226 1.00 34.81 ATOM 2618 CA ARG 1756 20.982 −20.969 10.302 1.00 34.68 ATOM 2619 CS ARG 1756 21.688 −21.100 8.959 1.00 34.78 ATOM 2620 CG ARG 1756 22.746 −22.179 8.910 1.00 35.93 ATOM 2621 CD ARG 1756 23.297 −22.306 7.511 1.00 41.60 ATOM 2622 NE ARG 1756 23.786 −21.025 6.999 1.00 46.42 ATOM 2624 CZ ARG 1756 24.889 −20.419 7.427 1.00 48.38 ATOM 2625 NH1 ARG 1756 25.637 −20.976 8.381 1.00 48.10 ATOM 2628 NH2 ARG 1756 25.236 −19.242 6.909 1.00 46.62 ATOM 2631 C ARG 1756 22.002 −20.666 11.399 1.00 36.17 ATOM 2632 O ARG 1756 22.372 −21.541 12.177 1.00 38.33 ATOM 2633 N ILE 1757 22.433 −19.413 11.478 1.00 37.00 ATOM 2635 CA ILE 1757 23.416 −18.998 12.468 1.00 35.60 ATOM 2636 CS ILE 1757 23.964 −17.588 12.141 1.00 35.54 ATOM 2637 CG2 ILE 1757 24.921 −17.131 13.217 1.00 32.41. ATOM 2638 CG1 ILE 1757 24.693 −17.612 10.794 1.00 33.77 ATOM 2639 CD1 ILE 1757 25.097 −16.253 10.287 1.00 33.49 ATOM 2640 C ILE 1757 22.866 −19.048 13.891 1.00 37.28 ATOM 2641 O ILE 1757 23.531 −19.556 14.779 1.00 38.42 ATOM 2642 N VAL 1758 21.634 −18.585 14.088 1.00 39.19 ATOM 2644 CA VAL 1758 21.016 −18.584 15.421 1.00 39.84 ATOM 2645 CS VAL 1758 19.560 −18.017 15.403 1.00 37.62 ATOM 2646 CG1 VAL 1758 18.918 −18.144 16.773 1.00 38.30 ATOM 2647 CG2 VAL 1758 19.560 −16.560 15.009 1.00 39.62 ATOM 2648 C VAL 1758 20.983 −19.997 15.988 1.00 41.98 ATOM 2649 O VAL 1758 21.380 −20.229 17.128 1.00 43.36 ATOM 2650 N ALA 1759 20.501 −20.932 15.182 1.00 43.31 ATOM 2652 CA ALA 1759 20.418 −22.325 15.589 1.00 44.00 ATOM 2653 CB ALA 1759 19.836 −23.150 14.459 1.00 44.52 ATOM 2654 C ALA 1759 21.784 −22.867 15.976 1.00 45.98 ATOM 2655 O ALA 1759 21.894 −23.725 16.841 1.00 48.78 ATOM 2656 N LEU 1760 22.823 −22.375 15.319 1.00 48.93 ATOM 2658 CA LEU 1760 24.175 −22.831 15.592 1.00 51.47 ATOM 2659 CB LEU 1760 24.954 −22.900 14.280 1.00 53.63 ATOM 2660 CG LEU 1760 24.284 −23.864 13.295 1.00 57.84 ATOM 2661 CD1 LEU 1760 24.993 −23.847 11.948 1.00 61.83 ATOM 2662 CD2 LEU 1760 24.260 −25.277 13.886 1.00 58.57 ATOM 2663 C LEU 1760 24.911 −21.965 16.607 1.00 53.60 ATOM 2664 O LEU 1760 26.078 −22.214 16.919 1.00 54.00 ATOM 2665 N THR 1761 24.222 −20.963 17.141 1.00 55.77 ATOM 2667 CA THR 1761 24.820 −20.060 18.111 1.00 56.64 ATOM 2668 CS THR 1761 24.250 −18.627 17.979 1.00 55.76 ATOM 2669 OG1 THR 1761 24.444 −18.154 16.644 1.00 56.20 ATOM 2671 CG2 THR 1761 24.962 −17.680 18.917 1.00 55.25 ATOM 2672 C THR 1761 24.636 −20.548 19.539 1.00 58.16 ATOM 2673 O THR 1762 23.566 −21.021 19.919 1.00 56.85 ATOM 2674 N SER 1762 25.706 −20.436 20.318 1.00 61.74 ATOM 2676 CA SER 1762 25.706 −20.833 21.717 1.00 64.50 ATOM 2677 CB SER 1762 27.155 −20.979 22.205 1.00 68.82 ATOM 2678 OG SER 1762 27.232 −21.544 23.508 1.00 73.15 ATOM 2680 C SER 1762 24.965 −19.775 22.547 1.00 63.87 ATOM 2681 O SER 1762 25.080 −18.563 22.296 1.00 63.22 ATOM 3420 PA PCP 400 62.748 10.301 7.817 1.00 90.90 ATOM 3421 O1A PCP 400 62.509 10.036 9.280 1.00 92.35 ATOM 3422 O2A PCP 400 61.832 11.180 7.038 1.00 90.49 ATOM 3423 O5* PCP 400 62.744 8.904 7.142 1.00 83.57 ATOM 3424 PB PCP 400 65.226 11.946 8.294 1.00 101.51 ATOM 3425 O1B PCP 400 65.246 13.015 7.264 1.00 102.85 ATOM 3426 O2B PCP 400 66.527 11.458 8.830 1.00 99.88 ATOM 3427 O3A PCP 400 64.334 10.725 7.584 1.00 96.64 ATOM 3428 C3B PCP 400 64.345 12.502 9.635 1.00 102.94 ATOM 3429 C5* PCP 400 62.337 8.684 5.839 1.00 71.21 ATOM 3430 C4* PCP 400 62.479 7.204 5.587 1.00 64.48 ATOM 3431 04* PCP 400 63.713 6.745 6.169 1.00 60.91 ATOM 3432 C1* PCP 400 63.394 5.459 6.680 1.00 54.96 ATOM 3433 N9 PCP 400 64.326 5.101 7.712 1.00 47.26 ATOM 3434 C4 PCP 400 65.017 3.903 7.840 1.00 46.24 ATOM 3435 N3 PCP 400 64.926 2.770 7.062 1.00 41.02 ATOM 3436 C2 PCP 400 65.802 1.878 7.531 1.00 40.72 ATOM 3437 N1 PCP 400 66.674 1.917 8.558 1.00 37.37 ATOM 3438 C6 PCP 400 66.735 3.028 9.305 1.00 40.23 ATOM 3439 N6 PCP 400 67.573 3.134 10.333 1.00 33.92 ATOM 3442 C5 PCP 400 65.862 4.091 8.937 1.00 44.12 ATOM 3443 N7 PCP 400 65.674 5.361 9.472 1.00 45.15 ATOM 3444 C8 PCP 400 64.761 5.894 8.702 1.00 44.83 ATOM 3445 C2* PCP 400 61.986 5.500 7.254 1.00 57.63 ATOM 3446 O2* PCP 400 61.454 4.153 7.211 1.00 56.45 ATOM 3448 C3* PCP 400 61.328 6.402 6.245 1.00 61.31 ATOM 3449 O3* PCP 400 60.689 5.644 5.206 1.00 64.65 ATOM 3451 PA PCP 401 9.366 9.801 17.743 0.50 74.43 ATOM 3452 O1A PCP 401 9.463 8.736 16.709 0.50 75.37 ATOM 3453 O2A PCP 401 10.330 10.926 17.699 0.50 75.86 ATOM 3454 O5* PCP 401 9.427 9.108 19.186 0.50 67.44 ATOM 3455 PB PCP 401 6.878 10.679 16.547 0.50 82.27 ATOM 3456 O1B PCP 401 6.223 11.982 16.778 0.50 82.91 ATOM 3457 O2B PCP 401 6.020 9.486 16.408 0.50 82.70 ATOM 3458 O3A PCP 401 7.868 10.423 17.814 0.50 78.30 ATOM 3459 C3B PCP 401 7.790 10.845 15.159 0.50 82.50 ATOM 3460 C5* PCP 401 10.184 9.593 20.275 0.50 54.44 ATOM 3461 C4* PCP 401 10.228 8.637 21.442 0.50 45.38 ATOM 3462 04* PCP 401 9.032 7.855 21.412 0.50 39.40 ATOM 3463 C1* PCP 401 9.397 6.509 21.641 0.50 35.00 ATOM 3464 N9 PCP 401 8.386 5.627 21.044 0.50 27.91 ATOM 3465 C4 PCP 401 7.790 4.469 21.564 0.50 23.36 ATOM 3466 N3 PCP 401 7.982 3.849 22.732 0.50 22.33 ATOM 3467 C2 PCP 401 7.239 2.768 22.838 0.50 20.26 ATOM 3468 N1 PCP 401 6.382 2.251 22.003 0.50 17.29 ATOM 3469 C6 PCP 401 6.202 2.877 20.856 0.50 19.35 ATOM 3470 N6 PCP 401 5.327 2.415 19.975 0.50 16.87 ATOM 3473 C5 PCP 401 6.932 4.038 20.603 0.50 21.72 ATOM 3474 N7 PCP 401 6.983 4.880 19.507 0.50 24.59 ATOM 3475 C8 PCP 401 7.847 5.786 19.832 0.50 24.26 ATOM 3476 C2* PCP 401 10.762 6.409 20.931 0.50 39.01 ATOM 3477 O2* PCP 401 11.609 5.326 21.412 0.50 43.88 ATOM 3479 C3* PCP 401 11.396 7.674 21.373 0.50 42.14 ATOM 3480 O3* PCP 401 11.918 7.515 22.681 0.50 44.21 ATOM 3482 N SER 461 78.844 26.057 14.057 1.00 43.87 ATOM 3484 CA SER 461 79.399 24.884 13.385 1.00 43.50 ATOM 3485 CB SER 461 78.488 23.655 13.616 1.00 39.99 ATOM 3486 C SER 461 79.572 25.181 11.888 1.00 42.14 ATOM 3487 O SER 461 79.473 24.292 11.038 1.00 40.29 ATOM 3488 N GLU 462 79.883 26.441 11.594 1.00 43.19 ATOM 3490 CA GLU 462 80.061 26.951 10.233 1.00 42.77 ATOM 3491 CB GLU 462 80.303 28.446 10.250 1.00 47.75 ATOM 3492 CG GLU 462 79.209 29.301 10.860 1.00 60.57 ATOM 3493 CD GLU 462 79.647 30.752 11.061 1.00 67.56 ATOM 3494 OE1 GLU 462 80.866 31.016 10.994 1.00 67.47 ATOM 3495 OE2 GLU 462 78.764 31.611 11.296 1.00 72.32 ATOM 3496 C GLU 462 81.207 26.357 9.457 1.00 39.55 ATOM 3497 O GLU 462 81.051 26.032 8.292 1.00 38.74 ATOM 3498 N TYR 463 82.375 26.299 10.091 1.00 36.47 ATOM 3500 CA TYR 463 83.567 25.806 9.420 1.00 34.19 ATOM 3501 CB TYR 463 84.702 26.828 9.505 1.00 35.55 ATOM 3502 CG TYR 463 84.393 28.059 8.675 1.00 42.11 ATOM 3503 CD1 TYR 463 84.004 29.264 9.283 1.00 43.15 ATOM 3504 CE1 TYR 463 83.619 30.361 8.513 1.00 42.40 ATOM 3505 CD2 TYR 463 84.395 27.990 7.280 1.00 39.78 ATOM 3506 CE2 TYR 463 84.012 29.078 6.509 1.00 39.04 ATOM 3507 CZ TYR 463 83.625 30.256 7.129 1.00 39.86 ATOM 3508 OH TYR 463 83.260 31.330 6.366 1.00 42.58 ATOM 3510 C TYR 463 84.055 24.434 9.800 1.00 33.28 ATOM 3511 O TYR 463 84.739 23.781 9.005 1.00 33.47 ATOM 3512 N GLU 464 83.695 23.976 10.993 1.00 34.42 ATOM 3514 CA GLU 464 84.117 22.660 11.444 1.00 36.38 ATOM 3515 CB GLU 464 85.618 22.663 11.750 1.00 40.90 ATOM 3516 CG GLU 464 86.041 23.755 12.729 1.00 46.29 ATOM 3517 CD GLU 464 87.548 23.810 12.943 1.00 51.33 ATOM 3518 OE1 GLU 464 87.970 24.247 14.038 1.00 54.49 ATOM 3519 OE2 GLU 464 88.312 23.430 12.025 1.00 53.18 ATOM 3520 C GLU 464 83.374 22.224 12.678 1.00 35.64 ATOM 3521 O GLU 464 83.111 23.052 13.555 1.00 37.40 ATOM 3522 N LEU 465 82.962 20.955 12.711 1.00 34.21 ATOM 3524 CA LEU 465 82.267 20.429 13.887 1.00 34.92 ATOM 3525 CB LEU 465 81.285 19.300 13.542 1.00 31.30 ATOM 3526 CG LEU 465 80.272 19.381 12.405 1.00 32.22 ATOM 3527 CD1 LEU 465 79.152 18.407 12.720 1.00 21.95 ATOM 3528 CD2 LEU 465 79.738 20.802 12.212 1.00 29.75 ATOM 3529 C LEU 465 83.326 19.855 14.814 1.00 36.17 ATOM 3530 O LEU 465 84.473 19.621 14.400 1.00 35.80 ATOM 3531 N PRO 466 82.970 19.629 16.083 1.00 36.20 ATOM 3532 CD PRO 466 81.722 20.018 16.758 1.00 38.17 ATOM 3533 CA PRO 466 83.925 19.072 17.037 1.00 36.06 ATOM 3534 CB PRO 466 83.132 19.035 18.333 1.00 35.57 ATOM 3535 CG PRO 466 82.185 20.194 18.171 1.00 38.67 ATOM 3536 C PRO 466 84.294 17.666 16.605 1.00 37.06 ATOM 3537 O PRO 466 83.498 16.959 15.979 1.00 34.50 ATOM 3538 N GLU 467 85.504 17.258 16.936 1.00 39.97 ATOM 3540 CA GLU 467 85.951 15.932 16.587 1.00 44.69 ATOM 3541 CB GLU 467 87.412 15.985 16.151 1.00 50.43 ATOM 3542 CG GLU 467 87.902 14.695 15.518 1.00 60.27 ATOM 3543 CD GLU 467 89.321 14.796 14.986 1.00 65.75 ATOM 3544 OE1 GLU 467 90.024 15.804 15.269 1.00 64.40 ATOM 3545 OE2 GLU 467 89.726 13.850 14.275 1.00 71.13 ATOM 3546 C GLU 467 85.775 15.002 17.783 1.00 43.30 ATOM 3547 O GLU 467 85.888 15.428 18.936 1.00 43.26 ATOM 3548 N ASP 468 85.433 13.750 17.504 1.00 43.09 ATOM 3550 CA ASP 468 85.254 12.739 18.545 1.00 44.15 ATOM 3551 CB ASP 468 83.785 12.614 18.979 1.00 44.54 ATOM 3552 CG ASP 468 83.574 11.562 20.072 1.00 41.84 ATOM 3553 OD1 ASP 468 82.405 11.244 20.368 1.00 39.81 ATOM 3554 OD2 ASP 468 84.570 11.057 20.636 1.00 42.92 ATOM 3555 C ASP 468 85.746 11.422 17.970 1.00 44.66 ATOM 3556 O ASP 468 84.982 10.663 17.368 1.00 44.56 ATOM 3557 N PRO 469 87.034 11.126 18.176 1.00 44.56 ATOM 3558 CD PRO 469 87.953 11.959 18.971 1.00 45.43 ATOM 3559 CA PRO 469 87.707 9.916 17.707 1.00 43.90 ATOM 3560 CB PRO 469 89.024 9.959 18.476 1.00 45.66 ATOM 3561 CG PRO 469 89.300 11.438 18.547 1.00 44.89 ATOM 3562 C PRO 469 86.934 8.627 17.971 1.00 42.60 ATOM 3563 O PRO 469 86.935 7.730 17.139 1.00 41.35 ATOM 3564 N ARG 470 86.229 8.569 19.096 1.00 43.25 ATOM 3566 CA ARG 470 85.460 7.380 19.470 1.00 44.81 ATOM 3567 CB ARG 470 84.722 7.612 20.789 1.00 48.36 ATOM 3568 CG ARG 470 85.579 8.201 21.889 1.00 53.41 ATOM 3569 CD ARG 470 84.764 8.458 23.138 1.00 55.42 ATOM 3570 NE ARG 470 83.581 9.261 22.861 1.00 58.57 ATOM 3572 CZ ARG 470 82.748 9.712 23.791 1.00 62.24 ATOM 3573 NH1 ARG 470 82.972 9.445 25.077 1.00 64.57 ATOM 3576 NH2 ARG 470 81.670 10.398 23.436 1.00 63.66 ATOM 3579 C ARG 470 84.439 6.924 18.437 1.00 43.69 ATOM 3580 O ARG 470 84.166 5.735 18.313 1.00 45.68 ATOM 3581 N TRP 471 83.879 7.866 17.693 1.00 42.41 ATOM 3583 CA TRP 471 82.851 7.534 16.720 1.00 38.92 ATOM 3584 CB TRP 471 81.577 8.268 17.095 1.00 35.80 ATOM 3585 CG TRP 471 80.967 7.741 18.335 1.00 37.13 ATOM 3586 CD2 TRP 471 80.158 6.569 18.443 1.00 37.26 ATOM 3587 CE2 TRP 471 79.723 6.483 19.785 1.00 38.20 ATOM 3588 CE3 TRP 471 79.748 5.582 17.530 1.00 35.59 ATOM 3589 CD1 TRP 471 81.010 8.300 19.584 1.00 36.42 ATOM 3590 NE1 TRP 471 80.260 7.553 20.462 1.00 35.89 ATOM 3592 CZ2 TRP 471 78.896 5.454 20.239 1.00 36.18 ATOM 3593 CZ3 TRP 471 78.934 4.561 17.978 1.00 32.81 ATOM 3594 CH2 TRP 471 78.514 4.505 19.321 1.00 34.82 ATOM 3595 C TRP 471 83.175 7.845 15.277 1.00 39.77 ATOM 3596 O TRP 471 82.478 7.391 14.362 1.00 39.56 ATOM 3597 N GLU 472 84.224 8.628 15.075 1.00 39.37 ATOM 3599 CA GLU 472 84.605 9.043 13.739 1.00 38.42 ATOM 3600 CB GLU 472 85.794 9.994 13.812 1.00 37.11 ATOM 3601 CG GLU 472 85.958 10.849 12.582 1.00 34.11 ATOM 3602 CD GLU 472 84.772 11.757 12.338 1.00 34.03. ATOM 3603 OE1 GLU 472 84.260 12.348 13.317 1.00 31.87 ATOM 3604 OE2 GLU 472 84.367 11.885 11.163 1.00 32.11 ATOM 3605 C GLU 472 84.910 7.901 12.791 1.00 39.78 ATOM 3606 O GLU 472 85.656 6.975 13.128 1.00 41.64 ATOM 3607 N LEU 473 84.303 7.958 11.610 1.00 37.71 ATOM 3609 CA LEU 473 84.538 6.957 10.590 1.00 36.94 ATOM 3610 CB LEU 473 83.258 6.196 10.265 1.00 35.38 ATOM 3611 CG LEU 473 83.438 5.065 9.236 1.00 37.67 ATOM 3612 CD1 LEU 473 84.070 3.845 9.903 1.00 37.28 ATOM 3613 CD2 LEU 473 82.106 4.687 8.598 1.00 37.87 ATOM 3614 C LEU 473 85.035 7.664 9.330 1.00 39.31 ATOM 3615 O LEU 473 84.484 8.697 8.938 1.00 40.55 ATOM 3616 N PRO 474 86.140 7.164 8.732 1.00 39.20 ATOM 3617 CD PRO 474 87.052 6.170 9.327 1.00 37.83 ATOM 3618 CA PRO 474 86.735 7.716 7.513 1.00 38.53 ATOM 3619 CB PRO 474 87.914 6.777 7.282 1.00 37.16 ATOM 3620 CG PRO 474 88.355 6.488 8.644 1.00 34.42 ATOM 3621 C PRO 474 85.733 7.607 6.370 1.00 40.25 ATOM 3622 O PRO 474 85.220 6.523 6.098 1.00 40.70 ATOM 3623 N ARG 475 85.492 8.723 5.685 1.00 41.09 ATOM 3625 CA ARG 475 84.534 8.746 4.590 1.00 42.26 ATOM 3626 CB ARG 475 84.487 10.132 3.948 1.00 39.19 ATOM 3627 CG ARG 475 83.957 11.199 4.876 1.00 35.19 ATOM 3628 CD ARG 475 84.074 12.593 4.301 1.00 30.76 ATOM 3629 NE ARG 475 83.796 13.567 5.345 1.00 22.86 ATOM 3631 CZ ARG 475 82.581 13.898 5.748 1.00 21.99 ATOM 3632 NH1 ARG 475 81.529 13.350 5.165 1.00 23.39 ATOM 3635 NH2 ARG 475 82.412 14.662 6.813 1.00 22.55 ATOM 3638 C ARG 475 84.838 7.692 3.538 1.00 45.38 ATOM 3639 O ARG 475 83.927 7.182 2.892 1.00 47.15 ATOM 3640 N ASP 476 86.106 7.319 3.390 1.00 47.13 ATOM 3642 CA ASP 476 86.461 6.325 2.387 1.00 51.33 ATOM 3643 CB ASP 476 87.973 6.294 2.134 1.00 55.23 ATOM 3644 CG ASP 476 88.768 5.841 3.340 1.00 61.16 ATOM 3645 OD1 ASP 476 88.863 4.617 3.573 1.00 65.55 ATOM 3646 OD2 ASP 476 89.331 6.713 4.036 1.00 65.78 ATOM 3647 C ASP 476 85.932 4.940 2.746 1.00 52.35 ATOM 3648 O ASP 476 85.815 4.063 1.885 1.00 55.49 ATOM 3649 N ARG 477 85.609 4.752 4.021 1.00 50.77 ATOM 3651 CA ARG 477 85.080 3.482 4.508 1.00 48.65 ATOM 3652 CB ARG 477 85.612 3.208 5.908 1.00 50.02 ATOM 3653 CG ARG 477 87.067 2.799 5.881 1.00 55.33 ATOM 3654 CD ARG 477 87.760 3.030 7.201 1.00 60.38 ATOM 3655 NE ARG 477 87.238 2.207 8.285 1.00 64.36 ATOM 3657 CZ ARG 477 87.748 2.203 9.513 1.00 69.16 ATOM 3658 NH1 ARG 477 88.794 2.968 9.814 1.00 70.73 ATOM 3661 NH2 ARG 477 87.190 1.459 10.459 1.00 71.59 ATOM 3664 C ARG 477 83.546 3.414 4.484 1.00 46.25 ATOM 3665 O ARG 477 82.957 2.481 5.013 1.00 46.36 ATOM 3666 N LEU 478 82.913 4.372 3.815 1.00 42.23 ATOM 3668 CA LEU 478 81.464 4.418 3.743 1.00 38.89 ATOM 3669 CB LEU 478 80.938 5.537 4.657 1.00 37.17 ATOM 3670 CG LEU 478 79.418 5.733 4.678 1.00 34.13 ATOM 3671 CD1 LEU 478 78.777 4.723 5.609 1.00 32.24 ATOM 3672 CD2 LEU 478 79.074 7.133 5.101 1.00 33.15 ATOM 3673 C LEU 478 81.059 4.697 2.303 1.00 38.34 ATOM 3674 O LEU 478 81.515 5.671 1.711 1.00 40.88 ATOM 3675 N VAL 479 80.208 3.850 1.738 1.00 37.34 ATOM 3677 CA VAL 479 79.763 4.042 0.364 1.00 37.61 ATOM 3678 CB VAL 479 80.105 2.829 −0.563 1.00 36.57 ATOM 3679 CG1 VAL 479 79.647 3.105 −1.994 1.00 31.59 ATOM 3680 CG2 VAL 479 81.608 2.567 −0.561 1.00 36.11 ATOM 3681 C VAL 479 78.267 4.277 0.375 1.00 39.24 ATOM 3682 O VAL 479 77.484 3.358 0.619 1.00 39.16 ATOM 3683 N LEU 480 77.894 5.528 0.142 1.00 41.32 ATOM 3685 CA LEU 480 76.505 5.960 0.123 1.00 41.60 ATOM 3686 CB LEU 480 76.446 7.480 −0.008 1.00 41.31 ATOM 3687 CG LEU 480 77.129 8.257 1.118 1.00 39.82 ATOM 3688 CD1 LEU 480 76.985 9.737 0.856 1.00 37.96. ATOM 3689 CD2 LEU 480 76.512 7.887 2.458 1.00 37.70 ATOM 3690 C LEU 480 75.733 5.312 −1.015 1.00 41.85 ATOM 3691 O LEU 480 76.235 5.224 −2.131 1.00 45.02 ATOM 3692 N GLY 481 74.501 4.897 −0.727 1.00 40.86 ATOM 3694 CA GLY 481 73.673 4.247 −1.727 1.00 40.21 ATOM 3695 C GLY 481 72.270 4.806 −1.873 1.00 39.78 ATOM 3696 O GLY 481 72.058 6.015 −1.810 1.00 41.68 ATOM 3697 N LYS 482 71.306 3.914 −2.063 1.00 39.98 ATOM 3699 CA LYS 482 69.910 4.297 −2.249 1.00 42.13 ATOM 3700 CB LYS 482 69.061 3.056 −2.566 1.00 42.73 ATOM 3701 C LYS 482 69.284 5.050 −1.084 1.00 43.13 ATOM 3702 O LYS 482 69.373 4.625 0.060 1.00 44.49 ATOM 3703 N PRO 483 68.676 6.204 −1.358 1.00 43.22 ATOM 3704 CD PRO 483 68.708 6.969 −2.613 1.00 44.40 ATOM 3705 CA PRO 483 68.044 6.973 −0.290 1.00 45.44 ATOM 3706 CB PRO 483 67.701 8.295 −0.980 1.00 45.01 ATOM 3707 CG PRO 483 67.573 7.923 −2.414 1.00 43.95 ATOM 3708 C PRO 483 66.801 6.261 0.232 1.00 47.67 ATOM 3709 O PRO 483 66.012 5.725 −0.547 1.00 46.76 ATOM 3710 N LEU 484 66.650 6.242 1.552 1.00 49.68 ATOM 3712 CA LEU 484 65.514 5.598 2.196 1.00 54.51 ATOM 3713 CB LEU 484 65.935 5.026 3.555 1.00 52.70 ATOM 3714 CG LEU 484 67.132 4.066 3.530 1.00 51.83 ATOM 3715 CD1 LEU 484 67.620 3.766 4.933 1.00 50.19 ATOM 3716 CD2 LEU 484 66.755 2.788 2.825 1.00 52.22 ATOM 3717 C LEU 484 64.317 6.554 2.357 1.00 58.82 ATOM 3718 O LEU 484 63.158 6.138 2.244 1.00 60.07 ATOM 3719 N GLY 485 64.599 7.831 2.609 1.00 61.91 ATOM 3721 CA GLY 485 63.538 8.810 2.778 1.00 65.89 ATOM 3722 C GLY 485 64.057 10.167 3.227 1.00 69.46 ATOM 3723 O GLY 485 65.230 10.301 3.597 1.00 70.65 ATOM 3724 N GLU 486 63.178 11.165 3.241 1.00 70.72 ATOM 3726 CA GLU 486 63.563 12.521 3.624 1.00 71.32 ATOM 3727 CB GLU 486 64.015 13.298 2.389 1.00 73.69 ATOM 3728 C GLU 486 62.435 13.269 4.312 1.00 70.93 ATOM 3729 O GLU 486 61.281 12.846 4.275 1.00 71.58 ATOM 3730 N GLY 487 62.781 14.404 4.909 1.00 70.10 ATOM 3732 CA GLY 487 61.798 15.211 5.603 1.00 68.11 ATOM 3733 C GLY 487 62.218 16.669 5.598 1.00 67.97 ATOM 3734 O GLY 487 62.938 17.109 4.696 1.00 67.68 ATOM 3735 N ALA 488 61.780 17.409 6.615 1.00 67.26 ATOM 3737 CA ALA 488 62.106 18.826 6.737 1.00 66.90 ATOM 3738 CB ALA 488 61.362 19.428 7.909 1.00 68.72 ATOM 3739 C ALA 488 63.607 19.004 6.921 1.00 67.08 ATOM 3740 O ALA 488 64.124 18.867 8.037 1.00 65.97 ATOM 3741 N PHE 489 64.297 19.248 5.806 1.00 66.76 ATOM 3743 CA PHE 489 65.754 19.439 5.773 1.00 65.91 ATOM 3744 CB PHE 489 66.134 20.794 6.379 1.00 66.45 ATOM 3745 C PHE 489 66.563 18.288 6.414 1.00 63.92 ATOM 3746 O PHE 489 67.622 18.503 7.031 1.00 63.16 ATOM 3747 N GLY 490 66.067 17.069 6.209 1.00 59.03 ATOM 3749 CA GLY 490 66.710 15.878 6.720 1.00 51.12 ATOM 3750 C GLY 490 66.619 14.823 5.638 1.00 48.59 ATOM 3751 O GLY 490 65.608 14.736 4.938 1.00 45.25 ATOM 3752 N GLN 491 67.659 14.003 5.525 1.00 48.77 ATOM 3754 CA GLN 491 67.732 12.951 4.519 1.00 47.40 ATOM 3755 CB GLN 491 68.529 13.474 3.319 1.00 49.92 ATOM 3756 CG GLN 491 68.653 12.514 2.155 1.00 56.31 ATOM 3757 CD GLN 491 69.604 13.020 1.088 1.00 58.79 ATOM 3758 OE1 GLN 491 70.043 14.171 1.130 1.00 59.63 ATOM 3759 NE2 GLN 491 69.929 12.161 0.122 1.00 59.05 ATOM 3762 C GLN 491 68.407 11.693 5.086 1.00 44.46 ATOM 3763 O GLN 491 69.396 11.782 5.806 1.00 44.15 ATOM 3764 N VAL 492 67.867 10.527 4.752 1.00 42.55 ATOM 3766 CA VAL 492 68.416 9.247 5.205 1.00 39.22 ATOM 3767 CB VAL 492 67.375 8.458 6.042 1.00 39.40 ATOM 3768 CG1 VAL 492 67.947 7.127 6.524 1.00 40.17 ATOM 3769 CG2 VAL 492 66.922 9.267 7.210 1.00 36.12 ATOM 3770 C VAL 492 68.746 8.396 3.975 1.00 37.57 ATOM 3771 O VAL 492 67.888 8.178 3.115 1.00 35.70 ATOM 3772 N VAL 493 69.990 7.961 3.845 1.00 36.27 ATOM 3774 CA VAL 493 70.333 7.127 2.711 1.00 37.61 ATOM 3775 CB VAL 493 71.237 7.863 1.643 1.00 37.45 ATOM 3776 CG1 VAL 493 70.836 9.319 1.524 1.00 38.29 ATOM 3777 CG2 VAL 493 72.717 7.713 1.943 1.00 36.53 ATOM 3778 C VAL 493 70.952 5.806 3.156 1.00 37.54 ATOM 3779 O VAL 493 71.542 5.711 4.233 1.00 37.32 ATOM 3780 N LEU 494 70.691 4.763 2.380 1.00 37.67 ATOM 3782 CA LEU 494 71.236 3.450 2.656 1.00 38.41 ATOM 3783 CB LEU 494 70.482 2.387 1.851 1.00 39.16 ATOM 3784 CG LEU 494 70.834 0.908 2.021 1.00 36.43 ATOM 3785 CD1 LEU 494 70.809 0.508 3.479 1.00 34.69 ATOM 3786 CD2 LEU 494 69.840 0.086 1.229 1.00 37.48 ATOM 3787 C LEU 494 72.683 3.541 2.202 1.00 39.30 ATOM 3788 O LEU 494 72.976 4.201 1.207 1.00 39.21 ATOM 3789 N ALA 495 73.584 2.922 2.954 1.00 40.08 ATOM 3791 CA ALA 495 74.996 2.954 2.619 1.00 41.70 ATOM 3792 CB ALA 495 75.654 4.162 3.283 1.00 41.63 ATOM 3793 C ALA 495 75.670 1.669 3.080 1.00 43.92 ATOM 3794 O ALA 495 75.033 0.818 3.711 1.00 45.20 ATOM 3795 N GLU 496 76.946 1.515 2.731 1.00 44.21 ATOM 3797 CA GLU 496 77.712 0.347 3.137 1.00 43.44 ATOM 3798 CE GLU 496 78.046 −0.538 1.943 1.00 45.87 ATOM 3799 CG GLU 496 76.816 −1.142 1.301 1.00 53.11 ATOM 3800 CD GLU 496 77.145 −2.262 0.339 1.00 56.68 ATOM 3801 OE1 GLU 496 76.473 −3.316 0.410 1.00 61.87 ATOM 3802 OE2 GLU 496 78.068 −2.091 −0.482 1.00 58.18 ATOM 3803 C GLU 496 78.973 0.773 3.860 1.00 40.97 ATOM 3804 O GLU 496 79.835 1.437 3.302 1.00 40.91 ATOM 3805 N ALA 497 79.036 0.439 5.136 1.00 42.07 ATOM 3807 CA ALA 497 80.173 0.786 5.959 1.00 43.69 ATOM 3808 CE ALA 497 79.709 1.104 7.366 1.00 40.90 ATOM 3809 C ALA 497 81.160 −0.372 5.962 1.00 46.16 ATOM 3810 O ALA 497 80.764 −1.525 5.814 1.00 46.90 ATOM 3811 N ILE 498 82.446 −0.059 6.090 1.00 48.78 ATOM 3813 CA ILE 498 83.494 −1.068 6.114 1.00 49.59 ATOM 3814 CE ILE 498 84.395 −0.993 4.858 1.00 49.46. ATOM 3815 CG2 ILE 498 85.524 −2.006 4.954 1.00 51.16 ATOM 3816 CG1 ILE 498 83.577 −1.244 3.591 1.00 48.96 ATOM 3817 CD1 ILE 498 82.924 0.009 2.998 1.00 52.50 ATOM 3818 C ILE 498 84.352 −0.877 7.355 1.00 51.33 ATOM 3819 O ILE 498 84.818 0.230 7.641 1.00 50.42 ATOM 3820 N GLY 499 84.506 −1.952 8.119 1.00 53.87 ATOM 3822 CA GLY 499 85.314 −1.909 9.324 1.00 58.16 ATOM 3823 C GLY 499 84.759 −1.094 10.483 1.00 62.44 ATOM 3824 O GLY 499 85.510 −0.400 11.175 1.00 65.17 ATOM 3825 N LEU 500 83.454 −1.187 10.720 1.00 62.92 ATOM 3827 CA LEU 500 82.839 −0.453 11.822 1.00 61.93 ATOM 3828 CE LEU 500 81.339 −0.752 11.888 1.00 58.77 ATOM 3829 CG LEU 500 80.501 −0.207 10.736 1.00 56.68 ATOM 3830 CD1 LEU 500 79.047 −0.547 10.964 1.00 55.05 ATOM 3831 CD2 LEU 500 80.682 1.298 10.635 1.00 56.30 ATOM 3832 C LEU 500 .83.501 −0.820 13.149 1.00 63.28 ATOM 3833 O LEU 500 83.623 −2.002 13.487 1.00 64.91 ATOM 3834 N PRO 505 87.387 −6.451 10.091 1.00 82.92 ATOM 3835 CD PRO 505 88.522 −6.966 10.874 1.00 83.74 ATOM 3836 CA PRO 505 87.618 −5.052 9.705 1.00 80.73 ATOM 3837 CB PRO 505 89.027 −4.770 10.247 1.00 81.95 ATOM 3838 CG PRO 505 89.655 −6.133 10.342 1.00 83.54 ATOM 3839 C PRO 505 87.514 −4.794 8.205 1.00 77.60 ATOM 3840 O PRO 505 87.445 −3.651 7.761 1.00 77.24 ATOM 3841 N ASN 506 87.488 −5.863 7.424 1.00 75.24 ATOM 3843 CA ASN 506 87.380 −5.727 5.981 1.00 72.92 ATOM 3844 CB ASN 506 88.435 −6.589 5.283 1.00 73.87 ATOM 3845 C ASN 506 85.978 −6.122 5.529 1.00 70.43 ATOM 3846 O ASN 506 85.719 −6.281 4.340 1.00 70.01 ATOM 3847 N ARG 507 85.075 −6.273 6.491 1.00 68.31 ATOM 3849 CA ARG 507 83.697 −6.647 6.200 1.00 65.59 ATOM 3850 CB ARG 507 83.112 −7.429 7.378 1.00 66.34 ATOM 3851 C ARG 507 82.846 −5.413 5.941 1.00 62.97 ATOM 3852 O ARG 507 83.191 −4.313 6.375 1.00 63.16 ATOM 3853 N VAL 508 81.740 −5.599 5.231 1.00 60.02 ATOM 3855 CA VAL 508 80.840 −4.495 4.947 1.00 58.59 ATOM 3856 CE VAL 508 80.532 −4.357 3.439 1.00 58.40 ATOM 3857 CG1 VAL 508 81.813 −4.196 2.658 1.00 61.14 ATOM 3858 CG2 VAL 508 79.751 −5.553 2.938 1.00 61.01 ATOM 3859 C VAL 508 79.537 −4.682 5.707 1.00 57.24 ATOM 3860 O VAL 508 79.031 −5.803 5.836 1.00 58.42 ATOM 3861 N THR 509 79.020 −3.579 6.237 1.00 54.22 ATOM 3863 CA THR 509 77.769 −3.572 6.973 1.00 48.99 ATOM 3864 CB THR 509 77.971 −3.100 8.428 1.00 49.59 ATOM 3865 OG1 THR 509 78.932 −3.935 9.082 1.00 51.71 ATOM 3867 CG2 THR 509 76.665 −3.166 9.198 1.00 50.69 ATOM 3868 C THR 509 76.837 −2.606 6.253 1.00 46.51 ATOM 3869 O THR 509 77.231 −1.503 5.886 1.00 44.91 ATOM 3870 N LYS 510 75.628 −3.059 5.966 1.00 45.65 ATOM 3872 CA LYS 510 74.658 −2.208 5.314 1.00 43.61 ATOM 3873 CB LYS 510 73.598 −3.058 4.632 1.00 45.46 ATOM 3874 CG LYS 510 72.845 −2.306 3.568 1.00 54.00 ATOM 3875 CD LYS 510 73.022 −2.912 2.183 1.00 58.74 ATOM 3876 CE LYS 510 72.194 −4.184 2.007 1.00 59.63. ATOM 3877 NZ LYS 510 72.711 −5.323 2.815 1.00 61.62 ATOM 3881 C LYS 510 74.065 −1.359 6.450 1.00 42.05 ATOM 3882 O LYS 510 73.566 −1.898 7.439 1.00 41.29 ATOM 3883 N VAL 511 74.185 −0.038 6.333 1.00 40.14 ATOM 3885 CA VAL 511 73.719 0.894 7.359 1.00 35.38 ATOM 3886 CE VAL 511 74.932 1.554 8.074 1.00 33.16 ATOM 3887 CG1 VAL 511 75.761 0.501 8.795 1.00 29.24 ATOM 3888 CG2 VAL 511 75.804 2.295 7.054 1.00 30.37 ATOM 3889 C VAL 511 72.856 2.005 6.776 1.00 33.90 ATOM 3890 O VAL 511 72.722 2.110 5.558 1.00 32.53 ATOM 3891 N ALA 512 72.261 2.813 7.655 1.00 31.97 ATOM 3893 CA ALA 512 71.434 3.956 7.248 1.00 31.10 ATOM 3894 CE ALA 512 70.088 3.945 7.952 1.00 27.38 ATOM 3895 C ALA 512 72.225 5.186 7.660 1.00 30.49 ATOM 3896 O ALA 512 72.775 5.235 8.766 1.00 30.10 ATOM 3897 N VAL 513 72.312 6.162 6.765 1.00 30.50 ATOM 3899 CA VAL 513 73.064 7.382 7.041 1.00 29.68 ATOM 3900 CE VAL 513 74.204 7.593 6.015 1.00 28.89 ATOM 3901 CG1 VAL 513 74.966 8.856 6.334 1.00 26.30 ATOM 3902 CG2 VAL 513 75.134. 6.389 5.987 1.00 26.66 ATOM 3903 C VAL 513 72.171 8.607 7.012 1.00 28.50 ATOM 3904 O VAL 513 71.536 8.893 5.994 1.00 26.27 ATOM 3905 N LYS 514 72.091 9.282 8.154 1.00 29.18 ATOM 3907 CA LYS 514 71.307 10.508 8.295 1.00 31.52 ATOM 3908 CE LYS 514 70.797 10.659 9.728 1.00 33.52 ATOM 3909 CG LYS 514 69.890 9.540 10.198 1.00 35.67 ATOM 3910 CD LYS 514 69.439 9.831 11.618 1.00 44.89 ATOM 3911 CE LYS 514 68.313 8.909 12.060 1.00 51.12 ATOM 3912 NZ LYS 514 67.029 9.137 11.307 1.00 57.11 ATOM 3916 C LYS 514 72.233 11.681 7.956 1.00 30.75 ATOM 3917 O LYS 514 73.390 11.698 8.379 1.00 30.08 ATOM 3918 N MET 515 71.724 12.651 7.201 1.00 29.45 ATOM 3920 CA MET 515 72.511 13.814 6.786 1.00 28.74 ATOM 3921 CB MET 515 73.342 13.466 5.552 1.00 27.72 ATOM 3922 CG MET 515 72.487 13.034 4.378 1.00 31.56 ATOM 3923 SD MET 515 73.442 12.549 2.945 1.00 34.98 ATOM 3924 CE MET 515 73.730 10.878 3.330 1.00 31.23 ATOM 3925 C MET 515 71.585 14.966 6.444 1.00 27.75 ATOM 3926 O MET 515 70.369 14.794 6.359 1.00 29.07 ATOM 3927 N LEU 516 72.152 16.145 6.247 1.00 28.33 ATOM 3929 CA LEU 516 71.348 17.313 5.912 1.00 31.16 ATOM 3930 CB LEU 516 72.052 18.605 6.339 1.00 28.70 ATOM 3931 CG LEU 516 72.312 18.866 7.826 1.00 28.33 ATOM 3932 CD1 LEU 516 73.098 20.156 7.949 1.00 28.45 ATOM 3933 CD2 LEU 516 71.020 18.959 8.604 1.00 21.64 ATOM 3934 C LEU 516 71.069 17.378 4.421 1.00 33.22 ATOM 3935 O LEU 516 71.762 16.760 3.619 1.00 35.00 ATOM 3936 N LYS 517 70.022 18.100 4.061 1.00 34.69 ATOM 3938 CA LYS 517 69.696 18.286 2.665 1.00 34.20 ATOM 3939 CB LYS 517 68.194 18.475 2.496 1.00 37.45 ATOM 3940 CG LYS 517 67.403 17.264 2.950 1.00 43.71 ATOM 3941 CD LYS 517 66.157 17.072 2.126 1.00 51.25 ATOM 3942 CE LYS 517 65.123 18.135 2.419 1.00 58.56 ATOM 3943 NZ LYS 517 64.010 18.049 1.438 1.00 63.12 ATOM 3947 C LYS 517 70.482 19.533 2.259 1.00 33.81 ATOM 3948 O LYS 517 70.991 20.244 3.130 1.00 33.17 ATOM 3949 N SER 518 70.603 19.788 0.959 1.00 33.42 ATOM 3951 CA SER 518 71.369 20.938 0.472 1.00 33.33 ATOM 3952 CB SER 518 71.550 20.842 −1.042 1.00 33.23 ATOM 3953 OG SER 518 70.306 20.624 −1.678 1.00 38.84 ATOM 3955 C SER 518 70.794 22.298 0.846 1.00 33.23 ATOM 3956 O SER 518 71.509 23.305 0.865 1.00 34.14 ATOM 3957 N ASP 519 69.510 22.313 1.178 1.00 32.77 ATOM 3959 CA ASP 519 68.825 23.541 1.570 1.00 33.26 ATOM 3960 CB ASP 519 67.401 23.563 0.995 1.00 35.10 ATOM 3961 CG ASP 519 66.484 22.503 1.617 1.00 38.98 ATOM 3962 OD1 ASP 519 66.958 21.430 2.042 1.00 37.30 ATOM 3963 OD2 ASP 519 65.261 22.754 1.674 1.00 43.65 ATOM 3964 C ASP 519 68.793 23.747 3.091 1.00 33.05 ATOM 3965 O ASP 519 68.114 24.648 3.580 1.00 35.19 ATOM 3966 N ALA 520 69.538 22.931 3.833 1.00 31.38 ATOM 3968 CA ALA 520 69.570 23.032 5.293 1.00 29.47 ATOM 3969 CB ALA 520 70.264 21.830 5.870 1.00 29.74 ATOM 3970 C ALA 520 70.229 24.301 5.812 1.00 29.83 ATOM 3971 O ALA 520 71.004 24.952 5.106 1.00 30.23 ATOM 3972 N THR 521 69.938 24.616 7.071 1.00 31.57 ATOM 3974 CA THR 521 70.487 25.793 7.742 1.00 34.56 ATOM 3975 CB THR 521 69.361 26.736 8.302 1.00 38.37 ATOM 3976 OG1 THR 521 68.670 26.082 9.376 1.00 41.75 ATOM 3978 CG2 THR 521 68.357 27.117 7.209 1.00 38.30 ATOM 3979 C THR 521 71.353 25.363 8.916 1.00 33.22 ATOM 3980 O THR 521 71.320 24.207 9.327 1.00 32.31 ATOM 3981 N GLU 522 72.092 26.310 9.479 1.00 34.43 ATOM 3983 CA GLU 522 72.951 26.042 10.619 1.00 39.53 ATOM 3984 CB GLU 522 73.634 27.340 11.068 1.00 46.35 ATOM 3985 CG GLU 522 74.398 27.271 12.402 1.00 58.03 ATOM 3986 CD GLU 522 75.772 26.603 12.301 1.00 63.14 ATOM 3987 OE1 GLU 522 76.800 27.321 12.404 1.00 61.75 ATOM 3988 OE2 GLU 522 75.824 25.359 12.158 1.00 66.35 ATOM 3989 C GLU 522 72.130 25.428 11.765 1.00 38.40 ATOM 3990 O GLU 522 72.642 24.622 12.543 1.00 37.92 ATOM 3991 N LYS 523 70.853 25.792 11.849 1.00 36.43 ATOM 3993 CA LYS 523 69.995 25.261 12.893 1.00 36.83 ATOM 3994 CB LYS 523 68.703 26.065 13.008 1.00 40.88 ATOM 3995 CG LYS 523 67.793 25.636 14.152 1.00 44.55 ATOM 3996 CD LYS 523 66.584 24.898 13.607 1.00 52.68 ATOM 3997 CE LYS 523 65.629 24.483 14.708 1.00 56.04 ATOM 3998 NZ LYS 523 64.537 23.646 14.123 1.00 58.13 ATOM 4002 C LYS 523 69.689 23.804 12.601 1.00 35.27 ATOM 4003 O LYS 523 69.645 22.985 13.513 1.00 36.58 ATOM 4004 N ASP 524 69.496 23.473 11.326 1.00 32.27 ATOM 4006 CA ASP 524 69.235 22.089 10.963 1.00 27.18 ATOM 4007 CB ASP 524 68.952 21.953 9.480 1.00 26.32 ATOM 4008 CG ASP 524 67.635 22.555 9.089 1.00 25.22 ATOM 4009 OD1 ASP 524 66.662 22.394 9.848 1.00 31.78 ATOM 4010 OD2 ASP 524 67.568 23.190 8.028 1.00 24.00 ATOM 4011 C ASP 524 70.445 21.268 11.342 1.00 26.83 ATOM 4012 O ASP 524 70.312 20.165 11.851 1.00 28.65 ATOM 4013 N LEU 525 71.633 21.827 11.129 1.00 28.69 ATOM 4015 CA LEU 525 72.872 21.148 11.473 1.00 26.96 ATOM 4016 CB LEU 525 74.077 21.981 11.049 1.00 22.80 ATOM 4017 CG LEU 525 75.445 21.355 11.341 1.00 22.32 ATOM 4018 CD1 LEU 525 75.522 19.883 10.858 1.00 18.89 ATOM 4019 CD2 LEU 525 76.504 22.212 10.704 1.00 17.44 ATOM 4020 C LEU 525 72.886 20.926 12.980 1.00 28.00 ATOM 4021 O LEU 525 73.160 19.816 13.462 1.00 28.82 ATOM 4022 N SER 526 72.567 21.992 13.707 1.00 27.98 ATOM 4024 CA SER 526 72.496 21.994 15.168 1.00 30.78 ATOM 4025 CB SER 526 71.939 23.345 15.627 1.00 33.18 ATOM 4026 OG SER 526 71.624 23.347 17.009 1.00 42.73 ATOM 4028 C SER 526 71.599 20.865 15.704 1.00 30.56 ATOM 4029 O SER 526 71.906 20.206 16.716 1.00 31.92 ATOM 4030 N ASP 527 70.484 20.665 15.018 1.00 28.19 ATOM 4032 CA ASP 527 69.516 19.651 15.366 1.00 27.41 ATOM 4033 CB ASP 527 68.207 19.932 14.632 1.00 27.63 ATOM 4034 CG ASP 527 67.492 21.172 15.149 1.00 27.37 ATOM 4035 OD1 ASP 527 67.870 21.728 16.211 1.00 26.70 ATOM 4036 OD2 ASP 527 66.525 21.579 14.487 1.00 33.80 ATOM 4037 C ASP 527 70.007 18.241 15.063 1.00 27.36 ATOM 4038 O ASP 527 69.722 17.309 15.816 1.00 30.13 ATOM 4039 N LEU 528 70.716 18.077 13.952 1.00 25.76 ATOM 4041 CA LEU 528 71.245 16.765 13.588 1.00 25.29 ATOM 4042 CB LEU 528 71.777 16.771 12.143 1.00 23.65 ATOM 4043 CG LEU 528 72.283 15.432 11.574 1.00 25.86 ATOM 4044 CD1 LEU 528 71.234 14.341 11.770 1.00 23.35 ATOM 4045 CD2 LEU 528 72.652 15.566 10.102 1.00 17.46 ATOM 4046 C LEU 528 72.351 16.368 14.578 1.00 25.66 ATOM 4047 O LEU 528 72.418 15.210 15.015 1.00 24.02 ATOM 4048 N ILE 529 73.200 17.338 14.934 1.00 26.36 ATOM 4050 CA ILE 529 74.304 17.130 15.886 1.00 26.17 ATOM 4051 CB ILE 529 75.192 18.381 16.003 1.00 22.72 ATOM 4052 CG2 ILE 529 76.250 18.180 17.057 1.00 21.32 ATOM 4053 CG1 ILE 529 75.876 18.666 14.685 1.00 20.71 ATOM 4054 CD1 ILE 529 76.621 19.965 14.675 1.00 25.60 ATOM 4055 C ILE 529 73.756 16.835 17.283 1.00 29.87 ATOM 4056 O ILE 529 74.253 15.948 17.977 1.00 32.20 ATOM 4057 N SER 530 72.741 17.591 17.693 1.00 28.63 ATOM 4059 CA SER 530 72.143 17.381 18.991 1.00 32.21 ATOM 4060 CB SER 530 71.031 18.399 19.231 1.00 37.45 ATOM 4061 OG SER 530 70.065 18.342 18.195 1.00 49.52 ATOM 4063 C SER 530 71.598 15.956 19.075 1.00 30.96 ATOM 4064 O SER 530 71.728 15.301 20.105 1.00 33.05 ATOM 4065 N GLU 531 70.996 15.476 17.996 1.00 29.13 ATOM 4067 CA GLU 531 70.468 14.117 17.987 1.00 29.84 ATOM 4068 CB GLU 531 69.672 13.847 16.709 1.00 30.29 ATOM 4069 CG GLU 531 69.093 12.445 16.666 1.00 27.39 ATOM 4070 CD GLU 531 68.521 12.074 15.331 1.00 31.34 ATOM 4071 OE1 GLU 531 67.929 10.981 15.228 1.00 35.90 ATOM 4072 OE2 GLU 531 68.660 12.860 14.376 1.00 38.37 ATOM 4073 C GLU 531 71.600 13.081 18.109 1.00 28.48 ATOM 4074 O GLU 531 71.468 12.094 18.822 1.00 28.17 ATOM 4075 N MET 532 72.682 13.281 17.364 1.00 28.12 ATOM 4077 CA MET 532 73.832 12.376 17.409 1.00 27.64 ATOM 4078 CB MET 532 74.953 12.899 16.499 1.00 26.47 ATOM 4079 CG MET 532 76.267 12.125 16.601 1.00 22.25 ATOM 4080 SD MET 532 77.406 12.610 15.286 1.00 30.32 ATOM 4081 CE MET 532 77.613 14.366 15.661 1.00 20.92 ATOM 4082 C MET 532 74.339 12.328 18.832 1.00 27.87 ATOM 4083 O MET 532 74.640 11.267 19.364 1.00 30.31 ATOM 4084 N GLU 533 74.439 13.497 19.442 1.00 27.08 ATOM 4086 CA GLU 533 74.906 13.594 20.802 1.00 28.50 ATOM 4087 CB GLU 533 75.071 15.064 21.177 1.00 29.09 ATOM 4088 CG GLU 533 76.216 15.745 20.433 1.00 28.90 ATOM 4089 CD GLU 533 77.564 15.070 20.661 1.00 31.08 ATOM 4090 OE1 GLU 533 78.001 14.969 21.823 1.00 34.15 ATOM 4091 OE2 GLU 533 78.202 14.643 19.678 1.00 33.60 ATOM 4092 C GLU 533 73.981 12.850 21.774 1.00 29.91 ATOM 4093 O GLU 533 74.455 12.093 22.637 1.00 29.73 ATOM 4094 N MET 534 72.670 13.014 21.588 1.00 29.70 ATOM 4096 CA MET 534 71.692 12.346 22.444 1.00 27.97 ATOM 4097 CB MET 534 70.258 12.751 22.082 1.00 28.95 ATOM 4098 CG MET 534 69.311 12.594 23.278 0.50 29.62 PRT1 ATOM 4099 SD MET 534 67.538 12.682 22.961 0.50 29.87 PRT1 ATOM 4100 CE MET 534 67.269 14.452 22.795 0.50 31.07 PRT1 ATOM 4101 C MET 534 71.855 10.821 22.362 1.00 28.36 ATOM 4102 O MET 534 71.833 10.143 23.386 1.00 27.02 ATOM 4103 N MET 535 72.048 10.297 21.151 1.00 26.96 ATOM 4105 CA MET 535 72.239 8.861 20.947 1.00 26.63 ATOM 4106 CB MET 535 72.347 8.521 19.456 1.00 24.67 ATOM 4107 CG MET 535 71.089 8.778 18.659 1.00 23.15 ATOM 4108 SD MET 535 71.160 8.062 17.011 1.00 24.57 ATOM 4109 CE MET 535 71.251 9.486 16.023 1.00 24.79 ATOM 4110 C MET 535 73.498 8.390 21.669 1.00 27.66 ATOM 4111 O MET 535 73.564 7.259 22.164 1.00 28.83 ATOM 4112 N LYS 536 74.515 9.246 21.698 1.00 29.13 ATOM 4114 CA LYS 536 75.757 8.918 22.392 1.00 30.50 ATOM 4115 CB LYS 536 76.812 9.985 22.131 1.00 29.15 ATOM 4116 CG LYS 536 77.499 9.883 20.802 1.00 27.71 ATOM 4117 CD LYS 536 78.377 11.100 20.615 1.00 28.12 ATOM 4118 CE LYS 536 79.085 11.096 19.279 1.00 26.89 ATOM 4119 NZ LYS 536 79.688 12.436 19.077 1.00 27.54 ATOM 4123 C LYS 536 75.480 8.836 23.892 1.00 31.92 ATOM 4124 O LYS 536 75.921 7.908 24.559 1.00 31.19 ATOM 4125 N MET 537 74.742 9.814 24.409 1.00 34.02 ATOM 4127 CA MET 537 74.384 9.881 25.822 1.00 36.35 ATOM 4128 CB MET 537 73.648 11.197 26.083 1.00 43.33 ATOM 4129 CG MET 537 73.096 11.376 27.507 1.00 54.60 ATOM 4130 SD MET 537 71.426 10.674 27.856 1.00 67.38 ATOM 4131 CE MET 537 71.684 9.813 29.440 1.00 62.03 ATOM 4132 C MET 537 73.507 8.705 26.253 1.00 34.53 ATOM 4133 O MET 537 73.744 8.069 27.275 1.00 36.76 ATOM 4134 N ILE 538 72.496 8.425 25.454 1.00 32.24 ATOM 4136 CA ILE 538 71.568 7.367 25.757 1.00 29.88 ATOM 4137 CB ILE 538 70.396 7.384 24.757 1.00 26.98 ATOM 4138 CG2 ILE 538 69.582 6.096 24.842 1.00 27.93 ATOM 4139 CG1 ILE 538 69.527 8.614 25.036 1.00 22.58 ATOM 4140 CD1 ILE 538 68.399 8.787 24.058 1.00 24.58 ATOM 4141 C ILE 538 72.236 6.006 25.804 1.00 31.83 ATOM 4142 O ILE 538 71.983 5.227 26.713 1.00 36.32 ATOM 4143 N GLY 539 73.102 5.718 24.848 1.00 32.45 ATOM 4145 CA GLY 539 73.744 4.422 24.850 1.00 32.13 ATOM 4146 C GLY 539 72.974 3.380 24.056 1.00 33.83 ATOM 4147 O GLY 539 71.876 3.654 23.530 1.00 33.75 ATOM 4148 N LYS 540 73.539 2.173 24.010 1.00 33.36 ATOM 4150 CA LYS 540 72.980 1.054 23.256 1.00 37.04 ATOM 4151 CB LYS 540 74.110 0.181 22.709 1.00 39.21 ATOM 4152 CG LYS 540 74.865 0.893 21.623 1.00 48.72 ATOM 4153 CD LYS 540 75.818 0.009 20.850 1.00 56.84 ATOM 4154 CE LYS 540 76.225 0.693 19.516 1.00 62.14 ATOM 4155 NZ LYS 540 77.252 −0.102 18.805 1.00 71.02 ATOM 4159 C LYS 540 71.938 0.162 23.901 1.00 36.51 ATOM 4160 O LYS 540 71.963 −0.096 25.113 1.00 38.52 ATOM 4161 N HIS 541 71.017 −0.295 23.058 1.00 32.98 ATOM 4163 CA HIS 541 69.963 −1.230 23.424 1.00 31.20 ATOM 4164 CB HIS 541 68.779 −0.561 24.095 1.00 30.35 ATOM 4165 CG HIS 541 67.815 −1.540 24.694 1.00 32.56 ATOM 4166 CD2 HIS 541 67.737 −2.058 25.941 1.00 32.45 ATOM 4167 ND1 HIS 541 66.795 −2.124 23.974 1.00 29.22 ATOM 4169 CE1 HIS 541 66.134 −2.965 24.753 1.00 31.56 ATOM 4170 NE2 HIS 541 66.679 −2.932 25.957 1.00 32.22 ATOM 4172 C HIS 541 69.509 −1.937 22.152 1.00 32.00 ATOM 4173 O HIS 541 69.409 −1.324 21.095 1.00 32.84 ATOM 4174 N LYS 542 69.187 −3.222 22.273 1.00 33.61 ATOM 4176 CA LYS 542 68.786 −4.061 21.154 1.00 31.54 ATOM 4177 CB LYS 542 68.653 −5.516 21.596 1.00 33.94 ATOM 4178 CG LYS 542 68.322 −6.451 20.437 1.00 42.34 ATOM 4179 CD LYS 542 68.083 −7.885 20.856 1.00 47.57 ATOM 4180 CE LYS 542 67.634 −8.726 19.658 1.00 52.70 ATOM 4181 NZ LYS 542 67.402 −10.146 20.023 1.00 59.51 ATOM 4185 C LYS 542 67.495 −3.611 20.487 1.00 29.57 ATOM 4186 O LYS 542 67.268 −3.884 19.305 1.00 27.99 ATOM 4187 N ASN 543 66.649 −2.931 21.253 1.00 28.32 ATOM 4189 CA ASN 543 65.378 −2.476 20.714 1.00 28.86. ATOM 4190 CB ASN 543 64.231 −2.947 21.601 1.00 29.33 ATOM 4191 CG ASN 543 64.247 −4.452 21.811 1.00 29.64 ATOM 4192 OD1 ASN 543 64.437 −4.926 22.930 1.00 33.86 ATOM 4193 ND2 ASN 543 64.106 −5.206 20.732 1.00 28.02 ATOM 4196 C ASN 543 65.252 −0.983 20.378 1.00 29.69 ATOM 4197 O ASN 543 64.159 −0.413 20.457 1.00 30.02 ATOM 4198 N ILE 544 66.372 −0.357 20.011 1.00 27.35 ATOM 4200 CA ILE 544 66.382 1.046 19.593 1.00 25.95 ATOM 4201 CB ILE 544 66.898 2.030 20.706 1.00 25.56 ATOM 4202 CG2 ILE 544 66.148 1.819 22.037 1.00 21.06 ATOM 4203 CG1 ILE 544 68.406 1.901 20.902 1.00 25.61 ATOM 4204 CD1 ILE 544 68.952 2.818 21.976 1.00 25.89 ATOM 4205 C ILE 544 67.341 1.083 18.399 1.00 25.97 ATOM 4206 O ILE 544 68.126 0.152 18.227 1.00 25.69 ATOM 4207 N ILE 545 67.226 2.095 17.537 1.00 27.27 ATOM 4209 CA ILE 545 68.129 2.243 16.384 1.00 27.02 ATOM 4210 CB ILE 545 67.541 3.194 15.307 1.00 27.30 ATOM 4211 CG2 ILE 545 68.592 3.553 14.269 1.00 26.52 ATOM 4212 CG1 ILE 545 66.309 2.570 14.638 1.00 22.63 ATOM 4213 CD1 ILE 545 66.605 1.447 13.665 1.00 17.57 ATOM 4214 C ILE 545 69.383 2.873 16.979 1.00 28.55 ATOM 4215 O ILE 545 69.346 4.014 17.451 1.00 29.47 ATOM 4216 N ASN 546 70.482 2.123 16.965 1.00 30.90 ATOM 4218 CA ASN 546 71.748 2.564 17.560 1.00 29.56 ATOM 4219 CB ASN 546 72.497 1.365 18.159 1.00 26.32 ATOM 4220 CG ASN 546 71.732 0.695 19.281 1.00 23.81 ATOM 4221 OD1 ASN 546 71.580 1.252 20.362 1.00 27.34 ATOM 4222 ND2 ASN 546 71.267 −0.515 19.039 1.00 23.49 ATOM 4225 C ASN 546 72.700 3.330 16.653 1.00 30.99 ATOM 4226 O ASN 546 72.679 3.169 15.430 1.00 30.98 ATOM 4227 N LEU 547 73.543 4.148 17.286 1.00 32.29 ATOM 4229 CA LEU 547 74.570 4.948 16.610 1.00 30.93 ATOM 4230 CE LEU 547 75.043 6.076 17.542 1.00 25.97 ATOM 4231 CG LEU 547 76.075 7.088 17.021 1.00 22.12 ATOM 4232 CD1 LEU 547 75.553 7.815 15.765 1.00 22.10 ATOM 4233 CD2 LEU 547 76.415 8.089 18.112 1.00 18.67 ATOM 4234 C LEU 547 75.756 4.039 16.264 1.00 30.70 ATOM 4235 O LEU 547 76.284 3.361 17.137 1.00 34.46 ATOM 4236 N LEU 548 76.141 3.993 14.992 1.00 30.97 ATOM 4238 CA LEU 548 77.262 3.165 14.562 1.00 30.73 ATOM 4239 CB LEU 548 76.929 2.406 13.281 1.00 29.24 ATOM 4240 CG LEU 548 75.788 1.394 13.371 1.00 28.77 ATOM 4241 CD1 LEU 548 75.924 0.460 12.209 1.00 26.55 ATOM 4242 CD2 LEU 548 75.839 0.616 14.683 1.00 23.48 ATOM 4243 C LEU 548 78.522 3.982 14.347 1.00 33.00 ATOM 4244 O LEU 548 79.640 3.500 14.558 1.00 35.92 ATOM 4245 N GLY 549 78.351 5.215 13.901 1.00 32.52 ATOM 4247 CA GLY 549 79.503 6.051 13.673 1.00 32.76 ATOM 4248 C GLY 549 79.092 7.411 13.180 1.00 33.72 ATOM 4249 O GLY 549 77.895 7.707 13.092 1.00 35.01 ATOM 4250 N ALA 550 80.089 8.226 12.840 1.00 33.47 ATOM 4252 CA ALA 550 79.848 9.566 12.337 1.00 30.69 ATOM 4253 CB ALA 550 79.555 10.509 13.497 1.00 28.66 ATOM 4254 C ALA 550 81.022 10.099 11.523 1.00 30.41 ATOM 4255 O ALA 550 82.181 9.780 11.808 1.00 29.13 ATOM 4256 N CYS 551 80.695 10.817 10.446 1.00 30.29 ATOM 4258 CA CYS 551 81.675 11.490 9.584 1.00 28.44 ATOM 4259 CE CYS 551 81.432 11.214 8.096 1.00 27.25 ATOM 4260 SG CYS 551 81.639 9.508 7.566 1.00 28.89 ATOM 4261 C CYS 551 81.337 12.950 9.883 1.00 27.07 ATOM 4262 O CYS 551 80.293 13.441 9.467 1.00 29.86 ATOM 4263 N THR 552 82.184 13.616 10.658 1.00 25.10 ATOM 4265 CA THR 552 81.952 14.997 11.047 1.00 24.37 ATOM 4266 CB THR 552 81.959 15.091 12.569 1.00 27.67 ATOM 4267 OG1 THR 552 83.271 14.760 13.052 1.00 26.11 ATOM 4269 CG2 THR 552 80.951 14.120 13.164 1.00 30.41 ATOM 4270 C THR 552 83.003 15.980 10.557 1.00 24.51 ATOM 4271 O THR 552 82.804 17.194 10.604 1.00 21.56 ATOM 4272 N GLN 553 84.151 15.441 10.162 1.00 27.13 ATOM 4274 CA GLN 553 85.284 16.243 9.710 1.00 26.64 ATOM 4275 CE GLN 553 86.592 15.679 10.283 1.00 25.24 ATOM 4276 CG GLN 553 86.641 15.561 11.809 1.00 22.38 ATOM 4277 CD GLN 553 86.464 16.897 12.515 1.00 24.04 ATOM 4278 OE1 GLN 553 87.267 17.815 12.344 1.00 31.50 ATOM 4279 NE2 GLN 553 85.403 17.017 13.304 1.00 21.59 ATOM 4282 C GLN 553 85.384 16.276 8.206 1.00 28.02 ATOM 4283 O GLN 553 85.069 15.293 7.537 1.00 30.20 ATOM 4284 N ASP 554 85.794 17.430 7.695 1.00 28.08 ATOM 4286 CA ASP 554 86.000 17.652 6.263 1.00 30.14 ATOM 4287 CE ASP 554 87.330 17.034 5.833 1.00 29.82 ATOM 4288 CG ASP 554 88.451 17.470 6.707 1.00 31.79 ATOM 4289 OD1 ASP 554 88.699 18.666 6.767 1.00 36.45 ATOM 4290 OD2 ASP 554 89.066 16.623 7.364 1.00 33.06 ATOM 4291 C ASP 554 84.895 17.217 5.317 1.00 29.52 ATOM 4292 O ASP 554 85.128 16.411 4.424 1.00 33.67 ATOM 4293 N GLY 555 83.709 17.793 5.488 1.00 29.02 ATOM 4295 CA GLY 555 82.586 17.476 4.621 1.00 26.05 ATOM 4296 C GLY 555 81.286 17.447 5.405 1.00 23.80 ATOM 4297 O GLY 555 81.269 17.751 6.597 1.00 24.09 ATOM 4298 N PRO 556 80.175 17.117 4.740 1.00 23.29 ATOM 4299 CD PRO 556 80.094 16.804 3.304 1.00 18.93 ATOM 4300 CA PRO 556 78.860 17.045 5.378 1.00 23.45 ATOM 4301 CB PRO 556 77.943 16.643 4.226 1.00 22.35 ATOM 4302 CG PRO 556 78.889 15.931 3.261 1.00 24.94 ATOM 4303 C PRO 556 78.806 16.019 6.503 1.00 26.66 ATOM 4304 O PRO 556 79.488 14.984 6.464 1.00 27.76 ATOM 4305 N LEU 557 78.006 16.324 7.522 1.00 29.14 ATOM 4307 CA LEU 557 77.842 15.440 8.676 1.00 30.83 ATOM 4308 CB LEU 557 77.173 16.181 9.842 1.00 28.40 ATOM 4309 CG LEU 557 76.775 15.393 11.097 1.00 22.93 ATOM 4310 CD1 LEU 557 77.989 14.897 11.835 1.00 23.02 ATOM 4311 CD2 LEU 557 75.970 16.285 11.984 1.00 23.53 ATOM 4312 C LEU 557 77.028 14.200 8.321 1.00 31.04 ATOM 4313 O LEU 557 75.968 14.293 7.694 1.00 31.89 ATOM 4314 N TYR 558 77.552 13.041 8.700 1.00 29.88 ATOM 4316 CA TYR 558 76.891 11.773 8.460 1.00 27.80 ATOM 4317 CB TYR 558 77.741 10.878 7.562 1.00 28.04 ATOM 4318 CG TYR 558 77.895 11.339 6.122 1.00 29.98 ATOM 4319 CD1 TYR 558 78.843 10.751 5.289 1.00 31.81 ATOM 4320 CE1 TYR 558 78.980 11.140 3.956 1.00 32.22 ATOM 4321 CD2 TYR 558 77.086 12.335 5.584 1.00 31.50 ATOM 4322 CE2 TYR 558 77.214 12.729 4.256 1.00 31.57 ATOM 4323 CZ TYR 558 78.166 12.125 3.449 1.00 32.04 ATOM 4324 OH TYR 558 78.317 12.511 2.134 1.00 33.34 ATOM 4326 C TYR 558 76.715 11.099 9.809 1.00 27.34 ATOM 4327 O TYR 558 77.678 10.937 10.558 1.00 25.80 ATOM 4328 N VAL 559 75.464 10.798 10.147 1.00 28.06 ATOM 4330 CA VAL 559 75.118 10.118 11.394 1.00 26.67 ATOM 4331 CB VAL 559 73.930 10.816 12.129 1.00 26.22 ATOM 4332 CG1 VAL 559 73.590 10.079 13.425 1.00 22.58 ATOM 4333 CG2 VAL 559 74.298 12.278 12.440 1.00 23.09 ATOM 4334 C VAL 559 74.745 8.715 10.943 1.00 24.32 ATOM 4335 O VAL 559 73.665 8.464 10.412 1.00 26.37 ATOM 4336 N ILE 560 75.689 7.815 11.095 1.00 23.63 ATOM 4338 CA ILE 560 75.514 6.448 10.664 1.00 24.67 ATOM 4339 CB ILE 560 76.901 5.859 10.299 1.00 24.62 ATOM 4340 CG2 ILE 560 76.753 4.507 9.646 1.00 30.13 ATOM 4341 CG1 ILE 560 77.627 6.810 9.326 1.00 21.87 ATOM 4342 CD1 ILE 560 79.114 6.538 9.162 1.00 22.25 ATOM 4343 C ILE 560 74.814 5.621 11.737 1.00 27.30 ATOM 4344 O ILE 560 75.306 5.505 12.865 1.00 28.80 ATOM 4345 N VAL 561 73.641 5.090 11.406 1.00 26.80 ATOM 4347 CA VAL 561 72.894 4.272 12.352 1.00 26.16 ATOM 4348 CB VAL 561 71.572 4.953 12.810 1.00 24.10 ATOM 4349 CG1 VAL 561 71.866 6.208 13.599 1.00 24.11 ATOM 4350 CG2 VAL 561 70.676 5.254 11.625 1.00 21.97 ATOM 4351 C VAL 561 72.572 2.901 11.761 1.00 27.98 ATOM 4352 O VAL 561 72.853 2.632 10.584 1.00 26.49 ATOM 4353 N GLU 562 71.998 2.039 12.599 1.00 28.86 ATOM 4355 CA GLU 562 71.605 0.685 12.219 1.00 28.23 ATOM 4356 CB GLU 562 71.090 −0.068 13.440 1.00 25.86 ATOM 4357 CG GLU 562 72.170 −0.392 14.424 1.00 27.04 ATOM 4358 CD GLU 562 71.641 −0.969 15.714 1.00 28.37 ATOM 4359 OE1 GLU 562 72.389 −1.714 16.372 1.00 33.36 ATOM 4360 OE2 GLU 562 70.491 −0.665 16.092 1.00 31.60 ATOM 4361 C GLU 562 70.529 0.720 11.171 1.00 29.67 ATOM 4362 O GLU 562 69.581 1.489 11.287 1.00 32.53 ATOM 4363 N TYR 563 70.666 −0.126 10.162 1.00 30.70 ATOM 4365 CA TYR 563 69.699 −0.209 9.083 1.00 30.65 ATOM 4366 CB TYR 563 70.419 −0.621 7.801 1.00 30.83 ATOM 4367 CG TYR 563 69.510 −0.905 6.633 1.00 32.10 ATOM 4368 CD1 TYR 563 68.545 0.018 6.236 1.00 33.24 ATOM 4369 CE1 TYR 563 67.715 −0.227 5.160 1.00 34.65 ATOM 4370 CD2 TYR 563 69.609 −2.098 5.922 1.00 31.04 ATOM 4371 CE2 TYR 563 68.779 −2.353 4.838 1.00 33.12 ATOM 4372 CZ TYR 563 67.831 −1.413 4.470 1.00 34.22 ATOM 4373 OH TYR 563 67.002 −1.650 3.400 1.00 34.76 ATOM 4375 C TYR 563 68.592 −1.223 9.406 1.00 34.39 ATOM 4376 O TYR 563 68.855 −2.325 9.884 1.00 34.87 ATOM 4377 N ALA 564 67.356 −0.861 9.091 1.00 35.49 ATOM 4379 CA ALA 564 66.212 −1.726 9.324 1.00 35.41 ATOM 4380 CB ALA 564 65.213 −1.000 10.210 1.00 35.93 ATOM 4381 C ALA 564 65.585 −2.056 7.962 1.00 37.19 ATOM 4382 O ALA 564 64.789 −1.276 7.434 1.00 38.08 ATOM 4383 N SER 565 65.931 −3.211 7.401 1.00 37.14 ATOM 4385 CA SER 565 65.433 −3.616 6.080 1.00 36.83 ATOM 4386 CB SER 565 66.151 −4.881 5.614 1.00 35.24 ATOM 4387 OG SER 565 66.105 −5.873 6.619 1.00 34.96 ATOM 4389 C SER 565 63.932 −3.782 5.886 1.00 38.65 ATOM 4390 O SER 565 63.428 −3.617 4.760 1.00 37.80 ATOM 4391 N LYS 566 63.212 −4.077 6.964 1.00 38.96 ATOM 4393 CA LYS 566 61.772 −4.271 6.851 1.00 37.83 ATOM 4394 CB LYS 566 61.357 −5.495 7.655 1.00 39.07 ATOM 4395 CG LYS 566 61.954 −6.765 7.078 1.00 43.73 ATOM 4396 CD LYS 566 61.813 −7.950 7.996 1.00 47.07 ATOM 4397 CE LYS 566 62.258 −9.216 7.299 1.00 47.77 ATOM 4398 NZ LYS 566 62.361 −10.326 8.278 1.00 51.48 ATOM 4402 C LYS 566 60.899 −3.050 7.165 1.00 37.53 ATOM 4403 O LYS 566 59.702 −3.180 7.442 1.00 38.55 ATOM 4404 N GLY 567 61.496 −1.866 7.066 1.00 35.23 ATOM 4406 CA GLY 567 60.788 −0.627 7.305 1.00 33.64 ATOM 4407 C GLY 567 60.120 −0.485 8.656 1.00 33.24 ATOM 4408 O GLY 567 60.518 −1.133 9.627 1.00 33.80 ATOM 4409 N ASN 568 59.120 0.389 8.716 1.00 31.65 ATOM 4411 CA ASN 568 58.407 0.623 9.952 1.00 33.38 ATOM 4412 CB ASN 568 57.831 2.055 10.025 1.00 37.10 ATOM 4413 CG ASN 568 56.624 2.272 9.116 1.00 37.78 ATOM 4414 OD1 ASN 568 55.552 1.708 9.337 1.00 41.15 ATOM 4415 ND2 ASN 568 56.780 3.147 8.124 1.00 35.74 ATOM 4418 C ASN 568 57.357 −0.435 10.263 1.00 33.33 ATOM 4419 O ASN 568 56.917 −1.178 9.384 1.00 32.54 ATOM 4420 N LEU 569 56.971 −0.490 11.532 1.00 33.35 ATOM 4422 CA LEU 569 56.004 −1.455 12.040 1.00 32.38 ATOM 4423 CB LEU 569 55.838 −1.263 13.552 1.00 27.50 ATOM 4424 CG LEU 569 54.954 −2.259 14.291 1.00 26.34 ATOM 4425 CD1 LEU 569 55.452 −3.671 14.007 1.00 24.19 ATOM 4426 CD2 LEU 569 54.968 −1.951 15.787 1.00 21.44 ATOM 4427 C LEU 569 54.641 −1.433 11.355 1.00 33.35 ATOM 4428 O LEU 569 54.060 −2.484 11.095 1.00 34.99 ATOM 4429 N ARG 570 54.130 −0.239 11.083 1.00 34.36 ATOM 4431 CA ARG 570 52.827 −0.091 10.445 1.00 36.82 ATOM 4432 CB ARG 570 52.548 1.393 10.188 1.00 37.28 ATOM 4433 CG ARG 570 51.210 1.689 9.539 1.00 43.90 ATOM 4434 CD ARG 570 51.212 3.099 8.967 1.00 50.39 ATOM 4435 NE ARG 570 52.273 3.268 7.973 1.00 54.99 ATOM 4437 CZ ARG 570 53.075 4.328 7.887 1.00 54.96 ATOM 4438 NH1 ARG 570 52.947 5.343 8.735 1.00 54.71 ATOM 4441 NH2 ARG 570 54.030 4.357 6.966 1.00 56.12 ATOM 4444 C ARG 570 52.818 −0.877 9.133 1.00 36.53 ATOM 4445 O ARG 570 51.968 −1.737 8.909 1.00 34.68 ATOM 4446 N GLU 571 53.830 −0.611 8.320 1.00 37.14 ATOM 4448 CA GLU 571 53.994 −1.253 7.031 1.00 37.94 ATOM 4449 CB GLU 571 55.126 −0.558 6.274 1.00 39.71 ATOM 4450 CG GLU 571 54.834 0.916 6.062 1.00 44.69 ATOM 4451 CD GLU 571 55.934 1.665 5.346 1.00 52.22 ATOM 4452 OE1 GLU 571 57.098 1.196 5.358 1.00 54.87 ATOM 4453 OE2 GLU 571 55.629 2.743 4.777 1.00 56.37 ATOM 4454 C GLU 571 54.258 −2.744 7.164 1.00 36.53 ATOM 4455 O GLU 571 53.692 −3.550 6.426 1.00 36.35 ATOM 4456 N TYR 572 55.105 −3.105 8.120 1.00 35.77 ATOM 4458 CA TYR 572 55.456 −4.499 8.371 1.00 36.28 ATOM 4459 CB TYR 572 56.446 −4.555 9.534 1.00 30.27 ATOM 4460 CG TYR 572 56.859 −5.925 10.006 1.00 31.65 ATOM 4461 CD1 TYR 572 57.889 −6.626 9.371 1.00 29.40 ATOM 4462 CE1 TYR 572 58.354 −7.839 9.883 1.00 29.32 ATOM 4463 CD2 TYR 572 56.292 −6.480 11.161 1.00 35.17 ATOM 4464 CE2 TYR 572 56.749 −7.696 11.680 1.00 33.08 ATOM 4465 CZ TYR 572 57.780 −8.366 11.038 1.00 35.15 ATOM 4466 OH TYR 572 58.234 −9.559 11.558 1.00 36.91 ATOM 4468 C TYR 572 54.189 −5.321 8.672 1.00 37.70 ATOM 4469 O TYR 572 53.942 −6.369 8.068 1.00 36.82 ATOM 4470 N LEU 573 53.368 −4.799 9.576 1.00 37.64 ATOM 4472 CA LEU 573 52.126 −5.442 9.970 1.00 36.03 ATOM 4473 CB LEU 573 51.497 −4.659 11.122 1.00 36.17 ATOM 4474 CG LEU 573 52.257 −4.641 12.445 1.00 36.39 ATOM 4475 CD1 LEU 573 51.590 −3.665 13.412 1.00 36.17 ATOM 4476 CD2 LEU 573 52.311 −6.042 13.032 1.00 32.13 ATOM 4477 C LEU 573 51.117 −5.562 8.822 1.00 36.33 ATOM 4478 O LEU 573 50.477 −6.596 8.649 1.00 35.19 ATOM 4479 N GLN 574 50.975 −4.502 8.038 1.00 37.66 ATOM 4481 CA GLN 574 50.024 −4.514 6.936 1.00 41.78 ATOM 4482 CB GLN 574 49.798 −3.103 6.413 1.00 43.82 ATOM 4483 CG GLN 574 48.898 −2.273 7.264 1.00 45.42 ATOM 4484 CD GLN 574 48.871 −0.850 6.801 1.00 49.56 ATOM 4485 OE1 GLN 574 49.456 −0.506 5.772 1.00 52.22 ATOM 4486 NE2 GLN 574 48.207 0.001 7.565 1.00 54.86 ATOM 4489 C GLN 574 50.401 −5.427 5.783 1.00 42.89 ATOM 4490 O GLN 574 49.532 −5.898 5.042 1.00 46.15 ATOM 4491 N ALA 575 51.695 −5.646 5.599 1.00 42.39 ATOM 4493 CA ALA 575 52.165 −6.516 4.532 1.00 40.19 ATOM 4494 CB ALA 575 53.597 −6.165 4.170 1.00 40.68 ATOM 4495 C ALA 575 52.088 −7.970 4.971 1.00 40.49 ATOM 4496 O ALA 575 52.437 −8.867 4.210 1.00 43.34 ATOM 4497 N ARG 576 51.630 −8.197 6.202 1.00 38.76 ATOM 4499 CA ARG 576 51.538 −9.542 6.761 1.00 38.44 ATOM 4500 CB ARG 576 52.600 −9.708 7.846 1.00 34.26 ATOM 4501 CG ARG 576 53.991 −9.609 7.284 1.00 37.16 ATOM 4502 CD ARG 576 55.052 −9.625 8.356 1.00 36.38 ATOM 4503 NE ARG 576 56.384 −9.663 7.760 1.00 36.98 ATOM 4505 CZ ARG 576 56.897 −8.714 6.983 1.00 38.62 ATOM 4506 NH1 ARG 576 56.204 −7.618 6.689 1.00 41.41 ATOM 4509 NH2 ARG 576 58.112 −8.863 6.491 1.00 37.48 ATOM 4512 C ARG 576 50.165 −9.860 7.321 1.00 40.55 ATOM 4513 O ARG 576 50.013 −10.746 8.169 1.00 43.20 ATOM 4514 N ARG 577 49.156 −9.146 6.844 1.00 41.98 ATOM 4516 CA ARG 577 47.794 −9.372 7.309 1.00 43.12 ATOM 4517 CB ARG 577 46.896 −8.226 6.851 1.00 44.21 ATOM 4518 CG ARG 577 47.206 −6.910 7.525 1.00 45.21 ATOM 4519 CD ARG 577 46.402 −5.766 6.941 1.00 47.50 ATOM 4520 NE ARG 577 46.172 −4.734 7.948 1.00 47.58 ATOM 4522 CZ ARG 577 45.447 −3.641 7.752 1.00 47.63 ATOM 4523 NH1 ARG 577 44.882 −3.421 6.574 1.00 49.05 ATOM 4526 NH2 ARG 577 45.256 −2.789 8.747 1.00 49.88 ATOM 4529 C ARG 577 47.241 −10.715 6.821 1.00 43.10 ATOM 4530 O ARG 577 47.297 −11.015 5.627 1.00 43.86 ATOM 4531 N GLN 594 53.448 −13.666 7.976 1.00 64.97 ATOM 4533 CA GLN 594 52.231 −13.872 8.759 1.00 66.30 ATOM 4534 CB GLN 594 51.419 −15.042 8.200 1.00 67.44 ATOM 4535 C GLN 594 52.582 −14.116 10.224 1.00 66.02 ATOM 4536 O GLN 594 53.162 −15.145 10.583 1.00 67.47 ATOM 4537 N LEU 595 52.218 −13.151 11.058 1.00 62.86 ATOM 4539 CA LEU 595 52.499 −13.187 12.480 1.00 59.77 ATOM 4540 CB LEU 595 52.597 −11.751 12.987 1.00 59.35 ATOM 4541 CG LEU 595 53.471 −10.905 12.051 1.00 61.70 ATOM 4542 CD1 LEU 595 53.307 −9.427 12.322 1.00 64.61 ATOM 4543 CD2 LEU 595 54.923 −11.324 12.175 1.00 62.38 ATOM 4544 C LEU 595 51.482 −13.985 13.290 1.00 57.49 ATOM 4545 O LEU 595 50.302 −14.026 12.951 1.00 56.36 ATOM 4546 N SER 596 51.969 −14.647 14.338 1.00 55.62 ATOM 4548 CA SER 596 51.134 −15.447 15.222 1.00 54.72 ATOM 4549 CB SER 596 51.905 −16.669 15.721 1.00 55.13 ATOM 4550 OG SER 596 52.871 −16.309 16.698 1.00 54.98 ATOM 4552 C SER 596 50.723 −14.597 16.415 1.00 54.73 ATOM 4553 O SER 596 51.348 −13.579 16.704 1.00 53.29 ATOM 4554 N SER 597 49.704 −15.051 17.137 1.00 55.09 ATOM 4556 CA SER 597 49.215 −14.337 18.307 1.00 56.44 ATOM 4557 CB SER 597 48.178 −15.185 19.044 1.00 59.14 ATOM 4558 OG SER 597 47.455 −16.009 18.138 1.00 65.57 ATOM 4560 C SER 597 50.387 −14.026 19.238 1.00 55.64 ATOM 4561 O SER 597 50.430 −12.966 19.856 1.00 56.04 ATOM 4562 N LYS 598 51.345 −14.948 19.315 1.00 54.91 ATOM 4564 CA LYS 598 52.528 −14.773 20.161 1.00 54.25 ATOM 4565 CB LYS 598 53.287 −16.096 20.311 1.00 54.23 ATOM 4566 CG LYS 598 54.236 −16.138 21.494 1.00 55.12 ATOM 4567 CD LYS 598 55.009 −17.448 21.523 1.00 59.41 ATOM 4568 CE LYS 598 55.711 −17.679 22.858 1.00 58.10 ATOM 4569 NZ LYS 598 54.750 −17.983 23.959 1.00 56.10 ATOM 4573 C LYS 598 53.439 −13.716 19.536 1.00 52.32 ATOM 4574 O LYS 598 53.986 −12.869 20.249 1.00 52.23 ATOM 4575 N ASP 599 53.573 −13.768 18.208 1.00 47.57 ATOM 4577 CA ASP 599 54.389 −12.818 17.466 1.00 45.47 ATOM 4578 CB ASP 599 54.324 −13.101 15.959 1.00 49.05 ATOM 4579 CG ASP 599 55.245 −14.238 15.525 1.00 54.16 ATOM 4580 OD1 ASP 599 56.242 −14.503 16.223 1.00 61.34 ATOM 4581 OD2 ASP 599 54.992 −14.863 14.471 1.00 55.80 ATOM 4582 C ASP 599 53.933 −11.383 17.721 1.00 43.55 ATOM 4583 O ASP 599 54.762 −10.491 17.895 1.00 44.34 ATOM 4584 N LEU 600 52.622 −11.160 17.751 1.00 39.73 ATOM 4586 CA LEU 600 52.104 −9.821 17.989 1.00 37.64 ATOM 4587 CB LEU 600 50.597 −9.743 17.719 1.00 35.42 ATOM 4588 CG LEU 600 50.075 −9.951 16.287 1.00 33.95 ATOM 4589 CD1 LEU 600 48.621 −9.552 16.262 1.00 36.59 ATOM 4590 CD2 LEU 600 50.841 −9.139 15.265 1.00 28.40 ATOM 4591 C LEU 600 52.429 −9.347 19.402 1.00 38.24 ATOM 4592 O LEU 600 52.817 −8.193 19.590 1.00 38.28 ATOM 4593 N VAL 601 52.305 −10.235 20.391 1.00 38.77 ATOM 4595 CA VAL 601 52.610 −9.855 21.772 1.00 38.87 ATOM 4596 CE VAL 601 52.121 −10.906 22.812 1.00 38.03 ATOM 4597 CG1 VAL 601 52.150 −10.303 24.223 1.00 36.21 ATOM 4598 CG2 VAL 601 50.710 −11.332 22.504 1.00 39.07 ATOM 4599 C VAL 601 54.123 −9.662 21.887 1.00 38.98 ATOM 4600 O VAL 601 54.601 −8.757 22.580 1.00 39.93 ATOM 4601 N SER 602 54.861 −10.488 21.155 1.00 37.35 ATOM 4603 CA SER 602 56.311 −10.422 21.126 1.00 37.11 ATOM 4604 CB SER 602 56.853 −11.469 20.154 1.00 39.38 ATOM 4605 OG SER 602 58.265 −11.413 20.061 1.00 46.76 ATOM 4607 C SER 602 56.695 −9.020 20.664 1.00 35.43 ATOM 4608 O SER 602 57.493 −8.339 21.315 1.00 35.01 ATOM 4609 N CYS 603 56.091 −8.586 19.561 1.00 33.42 ATOM 4611 CA CYS 603 56.329 −7.254 19.015 1.00 32.18 ATOM 4612 CE CYS 603 55.449 −7.035 17.790 1.00 32.38 ATOM 4613 SG CYS 603 55.440 −5.365 17.123 0.50 35.11 PRT1 ATOM 4614 C CYS 603 56.074 −6.167 20.059 1.00 31.20 ATOM 4615 O CYS 603 56.862 −5.234 20.185 1.00 32.44 ATOM 4616 N ALA 604 55.001 −6.321 20.828 1.00 29.74 ATOM 4618 CA ALA 604 54.640 −5.363 21.872 1.00 32.26 ATOM 4619 CE ALA 604 53.232 −5.675 22.412 1.00 31.75 ATOM 4620 C ALA 604 55.656 −5.365 23.019 1.00 33.71 ATOM 4621 O ALA 604 55.933 −4.326 23.621 1.00 33.49. ATOM 4622 N TYR 605 56.186 −6.544 23.326 1.00 35.56 ATOM 4624 CA TYR 605 57.176 −6.709 24.388 1.00 35.49 ATOM 4625 CE TYR 605 57.447 −8.206 24.617 1.00 36.12 ATOM 4626 CG TYR 605 58.562 −8.495 25.591 1.00 34.75 ATOM 4627 CD1 TYR 605 58.415 −8.237 26.954 1.00 34.30 ATOM 4628 CE1 TYR 605 59.444 −8.499 27.853 1.00 36.26 ATOM 4629 CD2 TYR 605 59.773 −9.021 25.150 1.00 37.39 ATOM 4630 CE2 TYR 605 60.812 −9.288 26.040 1.00 37.81 ATOM 4631 CZ TYR 605 60.641 −9.027 27.388 1.00 38.34 ATOM 4632 OH TYR 605 61.662 −9.324 28.265 1.00 42.09 ATOM 4634 C TYR 605 58.475 −5.972 24.027 1.00 34.98 ATOM 4635 O TYR 605 58.981 −5.171 24.822 1.00 35.83 ATOM 4636 N GLN 606 58.996 −6.247 22.828 1.00 33.99 ATOM 4638 CA GLN 606 60.218 −5.620 22.315 1.00 33.60 ATOM 4639 CB GLN 606 60.506 −6.111 20.894 1.00 31.37 ATOM 4640 CG GLN 606 60.858 −7.584 20.786 1.00 32.05 ATOM 4641 CD GLN 606 61.175 −8.015 19.354 1.00 30.33 ATOM 4642 OE1 GLN 606 62.145 −7.558 18.754 1.00 30.84 ATOM 4643 NE2 GLN 606 60.353 −8.895 18.810 1.00 33.75 ATOM 4646 C GLN 606 60.123 −4.079 22.321 1.00 34.86 ATOM 4647 O GLN 606 61.070 −3.390 22.702 1.00 37.54 ATOM 4648 N VAL 607 58.975 −3.555 21.904 1.00 32.89 ATOM 4650 CA VAL 607 58.748 −2.114 21.883 1.00 30.80 ATOM 4651 CE VAL 607 57.426 −1.777 21.120 1.00 28.82 ATOM 4652 CG1 VAL 607 57.121 −0.299 21.191 1.00 25.36 ATOM 4653 CG2 VAL 607 57.541 −2.204 19.661 1.00 23.37 ATOM 4654 C VAL 607 58.747 −1.532 23.312 1.00 30.48 ATOM 4655 O VAL 607 59.359 −0.486 23.563 1.00 29.42 ATOM 4656 N ALA 608 58.106 −2.225 24.255 1.00 30.07 ATOM 4658 CA ALA 608 58.064 −1.761 25.646 1.00 30.14 ATOM 4659 CE ALA 608 57.027 −2.548 26.452 1.00 28.49 ATOM 4660 C ALA 608 59.455 −1.849 26.305 1.00 31.25 ATOM 4661 O ALA 608 59.791 −1.054 27.198 1.00 28.90 ATOM 4662 N ARG 609 60.257 −2.819 25.870 1.00 31.61 ATOM 4664 CA ARG 609 61.608 −2.979 26.393 1.00 31.99 ATOM 4665 CE ARG 609 62.253 −4.245 25.856 1.00 34.93 ATOM 4666 CG ARG 609 61.606 −5.507 26.317 1.00 40.82 ATOM 4667 CD ARG 609 62.633 −6.606 26.397 1.00 42.68 ATOM 4668 NE ARG 609 63.275 −6.621 27.705 1.00 43.85 ATOM 4670 CZ ARG 609 64.332 −7.364 28.019 1.00 44.73 ATOM 4671 NH1 ARG 609 64.889 −8.162 27.108 1.00 41.40 ATOM 4674 NH2 ARG 609 64.803 −7.341 29.260 1.00 44.85 ATOM 4677 C ARG 609 62.459 −1.796 25.966 1.00 33.70 ATOM 4678 O ARG 609 63.130 −1.174 26.793 1.00 35.94 ATOM 4679 N GLY 610 62.459 −1.511 24.663 1.00 31.22 ATOM 4681 CA GLY 610 63.232 −0.391 24.157 1.00 27.21 ATOM 4682 C GLY 610 62.819 0.875 24.865 1.00 25.81 ATOM 4683 O GLY 610 63.665 1.652 25.300 1.00 26.21 ATOM 4684 N MET 611 61.511 1.056 25.015 1.00 27.12 ATOM 4686 CA MET 611 60.969 2.222 25.695 1.00 28.82 ATOM 4687 CB MET 611 59.457 2.288 25.524 1.00 29.29 ATOM 4688 CG MET 611 59.004 2.706 24.135 1.00 31.07 ATOM 4689 SD MET 611 59.732 4.286 23.617 1.00 28.38 ATOM 4690 CE MET 611 59.155 5.431 24.922 1.00 28.34 ATOM 4691 C MET 611 61.341 2.261 27.178 1.00 30.34 ATOM 4692 O MET 611 61.596 3.334 27.730 1.00 31.73 ATOM 4693 N GLU 612 61.347 1.109 27.837 1.00 32.72 ATOM 4695 CA GLU 612 61.723 1.057 29.253 1.00 35.46 ATOM 4696 CB GLU 612 61.603 −0.370 29.792 1.00 34.70 ATOM 4697 CG GLU 612 62.029 −0.516 31.237 1.00 32.31 ATOM 4698 CD GLU 612 62.135 −1.968 31.688 1.00 33.14 ATOM 4699 OE1 GLU 612 62.546 −2.834 30.883 1.00 30.79 ATOM 4700 OE2 GLU 612 61.826 −2.240 32.867 1.00 36.13 ATOM 4701 C GLU 612 63.178 1.544 29.353 1.00 36.43 ATOM 4702 O GLU 612 63.534 2.319 30.261 1.00 35.38 ATOM 4703 N TYR 613 63.999 1.107 28.391 1.00 35.47 ATOM 4705 CA TYR 613 65.403 1.507 28.334 1.00 33.16 ATOM 4706 CB TYR 613 66.156 0.743 27.241 1.00 31.33 ATOM 4707 CG TYR 613 67.612 1.146 27.132 1.00 33.03 ATOM 4708 CD1 TYR 613 68.584 0.544 27.931 1.00 36.69 ATOM 4709 CE1 TYR 613 69.930 0.927 27.851 1.00 36.82 ATOM 4710 CD2 TYR 613 68.021 2.148 26.247 1.00 33.49 ATOM 4711 CE2 TYR 613 69.352 2.540 26.157 1.00 34.73 ATOM 4712 CZ TYR 613 70.307 1.927 26.963 1.00 37.07 ATOM 4713 OH TYR 613 71.632 2.318 26.896 1.00 36.77 ATOM 4715 C TYR 613 65.539 3.005 28.088 1.00 31.82 ATOM 4716 O TYR 613 66.256 3.682 28.814 1.00 34.76 ATOM 4717 N LEU 614 64.836 3.536 27.090 1.00 28.44 ATOM 4719 CA LEU 614 64.931 4.956 26.793 1.00 25.67 ATOM 4720 CB LEU 614 64.089 5.319 25.569 1.00 24.75 ATOM 4721 CG LEU 614 64.545 4.778 24.208 1.00 23.73 ATOM 4722 CD1 LEU 614 63.594 5.257 23.125 1.00 20.54 ATOM 4723 CD2 LEU 614 65.983 5.213 23.894 1.00 23.21 ATOM 4724 C LEU 614 64.499 5.761 28.001 1.00 28.30 ATOM 4725 O LEU 614 65.110 6.770 28.345 1.00 27.09 ATOM 4726 N ALA 615 63.470 5.272 28.683 1.00 32.73 ATOM 4728 CA ALA 615 62.955 5.945 29.871 1.00 34.10 ATOM 4729 CB ALA 615 61.625 5.314 30.314 1.00 33.68 ATOM 4730 C ALA 615 63.986 5.913 31.007 1.00 33.84 ATOM 4731 O ALA 615 64.112 6.885 31.753 1.00 34.95 ATOM 4732 N SER 616 64.722 4.809 31.134 1.00 32.69 ATOM 4734 CA SER 616 65.738 4.703 32.175 1.00 33.50 ATOM 4735 CB SER 616 66.287 3.277 32.285 1.00 28.27 ATOM 4736 OG SER 616 67.076 2.935 31.165 1.00 25.54 ATOM 4738 C SER 616 66.870 5.678 31.865 1.00 35.43 ATOM 4739 O SER 616 67.637 6.061 32.755 1.00 37.32 ATOM 4740 N LYS 617 66.971 6.060 30.592 1.00 34.80 ATOM 4742 CA LYS 617 67.975 7.010 30.143 1.00 33.01 ATOM 4743 CB LYS 617 68.508 6.620 28.776 1.00 33.18 ATOM 4744 CG LYS 617 69.224 5.302 28.797 1.00 35.64 ATOM 4745 CD LYS 617 70.423 5.380 29.710 1.00 40.31 ATOM 4746 CE LYS 617 71.075 4.025 29.863 1.00 43.03 ATOM 4747 NZ LYS 617 72.426 4.152 30.449 1.00 45.54 ATOM 4751 C LYS 617 67.360 8.397 30.102 1.00 32.87 ATOM 4752 O LYS 617 67.892 9.308 29.470 1.00 34.06 ATOM 4753 N LYS 618 66.221 8.542 30.772 1.00 33.53 ATOM 4755 CA LYS 618 65.500 9.808 30.872 1.00 33.28 ATOM 4756 CB LYS 618 66.384 10.842 31.558 1.00 37.22 ATOM 4757 CG LYS 618 66.968 10.367 32.869 1.00 43.11 ATOM 4758 CD LYS 618 65.927 10.278 33.957 1.00 49.82 ATOM 4759 CE LYS 618 66.520 9.636 35.199 1.00 55.20 ATOM 4760 NZ LYS 618 65.669 9.853 36.415 1.00 61.31 ATOM 4764 C LYS 618 65.012 10.359 29.542 1.00 31.57 ATOM 4765 O LYS 618 64.651 11.530 29.455 1.00 31.10 ATOM 4766 N CYS 619 64.953 9.506 28.524 1.00 31.04 ATOM 4768 CA CYS 619 64.519 9.922 27.196 1.00 29.21 ATOM 4769 CB CYS 619 65.213 9.065 26.125 1.00 28.55 ATOM 4770 SG CYS 619 64.782 9.400 24.392 1.00 26.31 ATOM 4771 C CYS 619 62.999 9.849 27.051 1.00 30.91 ATOM 4772 O CYS 619 62.376 8.827 27.364 1.00 31.18 ATOM 4773 N ILE 620 62.411 10.967 26.632 1.00 29.48 ATOM 4775 CA ILE 620 60.981 11.073 26.416 1.00 29.34 ATOM 4776 CB ILE 620 60.402 12.344 27.060 1.00 28.12 ATOM 4777 CG2 ILE 620 58.944 12.535 26.645 1.00 28.76 ATOM 4778 CG1 ILE 620 60.521 12.267 28.581 1.00 28.36 ATOM 4779 CD1 ILE 620 60.062 13.522 29.270 1.00 25.55 ATOM 4780 C ILE 620 60.852 11.188 24.908 1.00 30.97 ATOM 4781 O ILE 620 61.254 12.193 24.336 1.00 33.88 ATOM 4782 N HIS 621 60.307 10.147 24.284 1.00 31.55 ATOM 4784 CA HIS 621 60.148 10.080 22.831 1.00 31.85 ATOM 4785 CB HIS 621 59.721 8.668 22.425 1.00 28.27 ATOM 4786 CG HIS 621 59.913 8.373 20.979 1.00 24.68 ATOM 4787 CD2 HIS 621 60.608 7.383 20.356 1.00 24.39 ATOM 4788 ND1 HIS 621 59.354 9.130 19.973 1.00 25.87 ATOM 4790 CE1 HIS 621 59.691 8.623 18.798 1.00 27.65 ATOM 4791 NE2 HIS 621 60.444 7.571 19.007 1.00 25.80 ATOM 4793 C HIS 621 59.187 11.096 22.224 1.00 34.38 ATOM 4794 O HIS 621 59.387 11.539 21.104 1.00 38.74 ATOM 4795 N ARG 622 58.080 11.374 22.898 1.00 37.17 ATOM 4797 CA ARG 622 57.093 12.346 22.425 1.00 37.27 ATOM 4798 CB ARG 622 57.718 13.746 22.298 1.00 38.63 ATOM 4799 CG ARG 622 58.261 14.271 23.601 1.00 40.47 ATOM 4800 CD ARG 622 58.661 15.739 23.530 1.00 44.76 ATOM 4801 NE ARG 622 59.129 16.174 24.842 1.00 52.09 ATOM 4803 CZ ARG 622 60.299 15.821 25.375 1.00 56.86 ATOM 4804 NH1 ARG 622 61.132 15.041 24.699 1.00 61.20 ATOM 4807 NH2 ARG 622 60.606 16.167 26.624 1.00 58.19 ATOM 4810 C ARG 622 56.324 11.994 21.151 1.00 37.23 ATOM 4811 O ARG 622 55.300 12.614 20.867 1.00 38.45 ATOM 4812 N ASP 623 56.805 11.035 20.364 1.00 36.55 ATOM 4814 CA ASP 623 56.075 10.652 19.160 1.00 36.52 ATOM 4815 CB ASP 623 56.581 11.403 17.910 1.00 39.68 ATOM 4816 CG ASP 623 55.635 11.247 16.687 1.00 48.75 ATOM 4817 OD1 ASP 623 56.077 11.491 15.538 1.00 49.98 ATOM 4818 OD2 ASP 623 54.445 10.879 16.872 1.00 49.65 ATOM 4819 C ASP 623 56.126 9.143 18.967 1.00 33.37 ATOM 4820 O ASP 623 56.325 8.650 17.864 1.00 31.77 ATOM 4821 N LEU 624 55.999 8.404 20.059 1.00 30.45 ATOM 4823 CA LEU 624 56.014 6.954 19.950 1.00 30.77 ATOM 4824 CB LEU 624 55.983 6.307 21.342 1.00 27.43 ATOM 4825 CG LEU 624 55.949 4.778 21.441 1.00 28.69 ATOM 4826 CD1 LEU 624 57.139 4.132 20.731 1.00 24.75 ATOM 4827 CD2 LEU 624 55.927 4.389 22.894 1.00 27.39 ATOM 4828 C LEU 624 54.803 6.532 19.109 1.00 31.22 ATOM 4829 O LEU 624 53.680 6.952 19.380 1.00 33.44 ATOM 4830 N ALA 625 55.053 5.763 18.054 1.00 28.85 ATOM 4832 CA ALA 625 54.009 5.286 17.159 1.00 26.93 ATOM 4833 CB ALA 625 53.559 6.400 16.227 1.00 25.03 ATOM 4834 C ALA 625 54.642 4.162 16.356 1.00 28.44 ATOM 4835 O ALA 625 55.863 4.065 16.317 1.00 31.32 ATOM 4836 N ALA 626 53.828 3.329 15.705 1.00 29.14 ATOM 4838 CA ALA 626 54.344 2.205 14.905 1.00 28.42 ATOM 4839 CB ALA 626 53.192 1.357 14.353 1.00 27.37 ATOM 4840 C ALA 626 55.231 2.698 13.771 1.00 26.38 ATOM 4841 O ALA 626 56.195 2.041 13.395 1.00 26.12 ATOM 4842 N ARG 627 54.890 3.861 13.230 1.00 27.16 ATOM 4844 CA ARG 627 55.669 4.474 12.158 1.00 28.44 ATOM 4845 CB ARG 627 55.022 5.794 11.733 1.00 28.19 ATOM 4846 CG ARG 627 54.889 6.793 12.867 1.00 30.34 ATOM 4847 CD ARG 627 54.456 8.155 12.361 1.00 34.08 ATOM 4848 NE ARG 627 54.081 9.024 13.471 1.00 35.58 ATOM 4850 CZ ARG 627 52.849 9.123 13.950 1.00 35.55 ATOM 4851 NH1 ARG 627 51.860 8.422 13.420 1.00 35.67 ATOM 4854 NH2 ARG 627 52.618 9.898 14.993 1.00 40.81 ATOM 4857 C ARG 627 57.108 4.733 12.630 1.00 28.06 ATOM 4858 O ARG 627 58.044 4.737 11.825 1.00 29.80 ATOM 4859 N ASN 628 57.272 4.935 13.940 1.00 28.50 ATOM 4861 CA ASN 628 58.582 5.195 14.544 1.00 26.14 ATOM 4862 CB ASN 628 58.494 6.340 15.551 1.00 23.55 ATOM 4863 CG ASN 628 58.319 7.681 14.874 1.00 27.48 ATOM 4864 OD1 ASN 628 58.874 7.919 13.800 1.00 34.12 ATOM 4865 ND2 ASN 628 57.543 8.556 15.479 1.00 23.21 ATOM 4868 C ASN 628 59.263 3.965 15.153 1.00 26.76 ATOM 4869 O ASN 628 60.202 4.078 15.948 1.00 26.90 ATOM 4870 N VAL 629 58.774 2..794 14.767 1.00 27.02 ATOM 4872 CA VAL 629 59.344 1.523 15.186 1.00 27.81 ATOM 4873 CB VAL 629 58.298 0.622 15.864 1.00 26.83 ATOM 4874 CG1 VAL 629 58.876 −0.766 16.115 1.00 20.74 ATOM 4875 CG2 VAL 629 57.836 1.259 17.165 1.00 22.49 ATOM 4876 C VAL 629 59.781 0.895 13.861 1.00 28.61 ATOM 4877 O VAL 629 58.983 0.809 12.924 1.00 28.76 ATOM 4878 N LEU 630 61.059 0.557 13.746 1.00 30.35 ATOM 4880 CA LEU 630 61.576 −0.033 12.514 1.00 32.42 ATOM 4881 CB LEU 630 62.824 0.725 12.040 1.00 32.28 ATOM 4882 CG LEU 630 62.697 2.249 11.880 1.00 27.75 ATOM 4883 CD1 LEU 630 64.019 2.860 11.469 1.00 24.71 ATOM 4884 CD2 LEU 630 61.611 2.582 10.872 1.00 27.70 ATOM 4885 C LEU 630 61.895 −1.488 12.799 1.00 32.89 ATOM 4886 O LEU 630 62.167 −1.838 13.943 1.00 32.32 ATOM 4887 N VAL 631 61.831 −2.336 11.774 1.00 34.81 ATOM 4889 CA VAL 631 62.087 −3.772 11.943 1.00 33.87 ATOM 4890 CB VAL 631 60.818 −4.616 11.597 1.00 31.60 ATOM 4891 CG1 VAL 631 60.929 −6.004 12.197 1.00 30.84. ATOM 4892 CG2 VAL 631 59.545 −3.916 12.089 1.00 25.53 ATOM 4893 C VAL 631 63.286 −4.256 11.109 1.00 34.95 ATOM 4894 O VAL 631 63.365 −4.009 9.892 1.00 37.01 ATOM 4895 N THR 632 64.215 −4.942 11.770 1.00 35.08 ATOM 4897 CA THR 632 65.418 −5.444 11.104 1.00 35.96 ATOM 4898 CB THR 632 66541 −5.711 12.116 1.00 34.29 ATOM 4899 OG1 THR 632 66.187 −6.818 12.953 1.00 32.35 ATOM 4901 CG2 THR 632 66.750 −4.488 12.985 1.00 33.42 ATOM 4902 C THR 632 65.162 −6.712 10.300 1.00 39.32 ATOM 4903 O THR 632 64.078 −7.302 10.382 1.00 41.24 ATOM 4904 N GLU 633 66.153 −7.123 9.511 1.00 42.32 ATOM 4906 CA GLU 633 66.030 −8.335 8.703 1.00 44.34 ATOM 4907 CB GLU 633 67.314 −8.609 7.912 1.00 46.06 ATOM 4908 CG GLU 633 67.205 −9.767 6.898 1.00 49.87 ATOM 4909 CD GLU 633 66.380 −9.445 5.629 1.00 53.04 ATOM 4910 OE1 GLU 633 65.637 −8.430 5.570 1.00 51.31 ATOM 4911 OE2 GLU 633 66.479 −10.226 4.667 1.00 55.48 ATOM 4912 C GLU 633 65.708 −9.526 9.600 1.00 44.58 ATOM 4913 O GLU 633 64.974 −10.423 9.207 1.00 46.56 ATOM 4914 N ASP 634 66.201 −9.493 10.833 1.00 44.12 ATOM 4916 CA ASP 634 65.961 −10.583 11.759 1.00 44.23 ATOM 4917 CB ASP 634 67.221 −10.867 12.580 1.00 50.17 ATOM 4918 CG ASP 634 68.443 −11.181 11.697 1.00 56.79 ATOM 4919 OD1 ASP 634 68.363 −12.113 10.857 1.00 59.62 ATOM 4920 OD2 ASP 634 69.482 −10.490 11.837 1.00 58.62 ATOM 4921 C ASP 634 64.756 −10.331 12.644 1.00 43.26 ATOM 4922 O ASP 634 64.652 −10.879 13.733 1.00 43.58 ATOM 4923 N ASN 635 63.858 −9.475 12.166 1.00 43.97 ATOM 4925 CA ASN 635 62.612 −9.126 12.847 1.00 43.66 ATOM 4926 CB ASN 635 61.698 −10.355 12.930 1.00 46.94 ATOM 4927 CG ASN 635 61.413 −10.958 11.572 1.00 48.19 ATOM 4928 OD1 ASN 635 60.831 −10.314 10.702 1.00 51.42 ATOM 4929 ND2 ASN 635 61.832 −12.198 11.380 1.00 49.44 ATOM 4932 C ASN 635 62.694 −8.463 14.216 1.00 43.03 ATOM 4933 O ASN 635 61.774 −8.596 15.031 1.00 43.03 ATOM 4934 N VAL 636 63.763 −7.712 14.467 1.00 42.69 ATOM 4936 CA VAL 636 63.915 −7.034 15.756 1.00 38.30 ATOM 4937 CB VAL 636 65.406 −6.861 16.134 1.00 37.92 ATOM 4938 CG1 VAL 636 65.555 −6.040 17.421 1.00 37.14 ATOM 4939 CG2 VAL 636 66.052 −8.226 16.306 1.00 37.55 ATOM 4940 C VAL 636 63.251 −5.673 15.688 1.00 35.75 ATOM 4941 O VAL 636 63.486 −4.926 14.746 1.00 36.28 ATOM 4942 N MET 637 62.355 −5.396 16.628 1.00 34.73 ATOM 4944 CA MET 637 61.672 −4.103 16.680 1.00 33.22 ATOM 4945 CB MET 637 60.456 −4.152 17.608 1.00 34.83 ATOM 4946 CG MET 637 59.364 −5.148 17.231 1.00 34.41 ATOM 4947 SD MET 637 58.661 −4.926 15.589 1.00 33.19 ATOM 4948 CE MET 637 58.869 −6.584 14.913 1.00 29.73 ATOM 4949 C MET 637 62.677 −3.107 17.250 1.00 33.75 ATOM 4950 O MET 637 63.281 −3.357 18.308 1.00 31.79 ATOM 4951 N LYS 638 62.839 −1.980 16.558 1.00 31.83 ATOM 4953 CA LYS 638 63.774 −0.939 16.965 1.00 28.17 ATOM 4954 CB LYS 638 64.986 −0.930 16.038 1.00 24.98 ATOM 4955 CG LYS 638 66.006 −1.967 16.400 1.00 23.17 ATOM 4956 CD LYS 638 67.193 −1.916 15.470 1.00 25.04 ATOM 4957 CE LYS 638 68.212 −2.969 15.847 1.00 24.79 ATOM 4958 NZ LYS 638 68.747 −2.765 17.220 1.00 24.91 ATOM 4962 C LYS 638 63.165 0.445 16.986 1.00 26.04 ATOM 4963 O LYS 638 62.803 0.958 15.936 1.00 24.44 ATOM 4964 N ILE 639 63.052 1.031 18.181 1.00 25.14 ATOM 4966 CA ILE 639 62.508 2.376 18.351 1.00 25.68 ATOM 4967 CB ILE 639 62.589 2.863 19.839 1.00 27.40 ATOM 4968 CG2 ILE 639 61.875 4.189 19.984 1.00 18.94 ATOM 4969 CG1 ILE 639 62.019 1.827 20.826 1.00 26.05 ATOM 4970 CD1 ILE 639 60.517 1.667 20.792 1.00 25.07 ATOM 4971 C ILE 639 63.387 3.338 17.543 1.00 25.82 ATOM 4972 O ILE 639 64.619 3.283 17.642 1.00 25.76 ATOM 4973 N ALA 640 62.758 4.231 16.783 1.00 25.92 ATOM 4975 CA ALA 640 63.477 5.218 15.976 1.00 26.12 ATOM 4976 CB ALA 640 63.222 4.964 14.506 1.00 26.54 ATOM 4977 C ALA 640 63.042 6.643 16.344 1.00 26.33 ATOM 4978 O ALA 640 61.996 6.828 16.974 1.00 26.20 ATOM 4979 N ASP 641 63.863 7.637 15.993 1.00 26.59 ATOM 4981 CA ASP 641 63.545 9.052 16.245 1.00 28.09 ATOM 4982 CB ASP 641 62.217 9.443 15.593 1.00 31.43 ATOM 4983 CG ASP 641 62.346 9.762 14.107 1.00 36.81 ATOM 4984 OD1 ASP 641 63.409 9.478 13.500 1.00 40.24 ATOM 4985 OD2 ASP 641 61.356 10.299 13.548 1.00 40.49 ATOM 4986 C ASP 641 63.455 9.442 17.700 1.00 28.40 ATOM 4987 O ASP 641 62.825 10.446 18.041 1.00 29.30 ATOM 4988 N PHE 642 64.080 8.658 18.564 1.00 30.27 ATOM 4990 CA PHE 642 64.044 8.943 19.992 1.00 30.97 ATOM 4991 CB PHE 642 64.327 7.664 20.787 1.00 24,64 ATOM 4992 CG PHE 642 65.673 7.063 20.505 1.00 20.96 ATOM 4993 CD1 PHE 642 66.812 7.539 21.163 1.00 16.89 ATOM 4994 CD2 PHE 642 65.806 6.026 19.576 1.00 16.23 ATOM 4995 CE1 PHE 642 68.072 6.990 20.900 1.00 18.35 ATOM 4996 CE2 PHE 642 67.051 5.471 19.305 1.00 18.76 ATOM 4997 CZ PHE 642 68.195 5.954 19.970 1.00 17.91 ATOM 4998 C PHE 642 65.024 10.045 20.414 1.00 34.53 ATOM 4999 O PHE 642 64.990 10.503 21.563 1.00 35.23 ATOM 5000 N GLY 643 65.910 10.433 19.500 1.00 36.40 ATOM 5002 CA GLY 643 66.888 11.455 19.799 1.00 38..28 ATOM 5003 C GLY 643 66.634 12.768 19.093 1.00 41.44 ATOM 5004 O GLY 643 67.482 13.652 19.132 1.00 44.10 ATOM 5005 N LEU 644 65.461 12.921 18.484 1.00 45.44 ATOM 5007 CA LEU 644 65.131 14.144 17.748 1.00 49.14 ATOM 5008 CB LEU 644 63.832 13.975 16.969 1.00 46.26 ATOM 5009 CG LEU 644 63.823 12.967 15.836 1.00 42.90 ATOM 5010 CD1 LEU 644 62.527 13.134 15.070 1.00 42.68 ATOM 5011 CD2 LEU 644 65.004 13.228 14.934 1.00 45.15 ATOM 5012 C LEU 644 65.027 15.396 18.605 1.00 53.90 ATOM 5013 O LEU 644 64.488 15.356 19.715 1.00 56.54 ATOM 5014 N ALA 645 65.534 16.505 18.068 1.00 57.59 ATOM 5016 CA ALA 645 65.505 17.794 18.759 1.00 60.15 ATOM 5017 CB ALA 645 66.539 18.741 18.156 1.00 59.55 ATOM 5018 C ALA 645 64.112 18.407 18.667 1.00 61.90 ATOM 5019 O ALA 645 63.393 18.500 19.663 1.00 63.83 ATOM 5020 N ASP 652 52.090 22.191 14.865 1.00 89.91 ATOM 5022 CA ASP 652 50.913 22.199 14.007 1.00 89.75 ATOM 5023 CB ASP 652 51.314 22.428 12.537 1.00 88.08 ATOM 5024 CG ASP 652 50.109 22.557 11.607 1.00 87.09 ATOM 5025 OD1 ASP 652 49.028 22.996 12.052 1.00 86.85 ATOM 5026 OD2 ASP 652 50.252 22.222 10.411 1.00 86.69 ATOM 5027 C ASP 652 50.145 20.890 14.156 1.00 89.98 ATOM 5028 O ASP 652 50.434 19.899 13.483 1.00 90.19 ATOM 5029 N TYR 653 49.145 20.905 15.027 1.00 90.26 ATOM 5031 CA TYR 653 48.318 19.730 15.277 1.00 90.78 ATOM 5032 CB TYR 653 47.272 20.048 16.344 1.00 91.65 ATOM 5033 CG TYR 653 47.804 20.185 17.755 1.00 93.43 ATOM 5034 CD1 TYR 653 47.017 20.757 18.752 1.00 94.60 ATOM 5035 CE1 TYR 653 47.477 20.885 20.058 1.00 95.35 ATOM 5036 CD2 TYR 653 49.083 19.738 18.101 1.00 93.46 ATOM 5037 CE2 TYR 653 49.558 19.860 19.406 1.00 94.36 ATOM 5038 CZ TYR 653 48.748 20.435 20.378 1.00 95.26 ATOM 5039 OH TYR 653 49.220 20.554 21.669 1.00 95.00 ATOM 5041 C TYR 653 47.602 19.231 14.021 1.00 90.47 ATOM 5042 O TYR 653 47.045 18.131 14.012 1.00 91.33 ATOM 5043 N TYR 654 47.632 20.031 12.962 1.00 89.21 ATOM 5045 CA TYR 654 46.954 19.673 11.727 1.00 89.09 ATOM 5046 CB TYR 654 46.205 20.893 11.188 1.00 88.23 ATOM 5047 CG TYR 654 45.275 21.499 12.209 1.00 87.65 ATOM 5048 CD1 TYR 654 45.776 22.140 13.343 1.00 86.76 ATOM 5049 CE1 TYR 654 44.929 22.655 14.312 1.00 87.17 ATOM 5050 CD2 TYR 654 43.895 21.396 12.067 1.00 88.61 ATOM 5051 CE2 TYR 654 43.032 21.912 13.033 1.00 89.32 ATOM 5052 CZ TYR 654 43.557 22.538 14.153 1.00 88.66 ATOM 5053 OH TYR 654 42.710 23.034 15.117 1.00 89.39 ATOM 5055 C TYR 654 47.857 19.080 10.651 1.00 89.49 ATOM 5056 O TYR 654 47.396 18.772 9.552 1.00 88.37 ATOM 5057 N LYS 655 49.139 18.919 10.959 1.00 90.80 ATOM 5059 CA LYS 655 50.056 18.356 9.982 1.00 93.18 ATOM 5060 CB LYS 655 51.508 18.713 10.311 1.00 95.66 ATOM 5061 CG LYS 655 52.504 18.133 9.315 1.00 99.82 ATOM 5062 CD LYS 655 53.932 18.585 9.562 1.00 103.58 ATOM 5063 CE LYS 655 54.898 17.833 8.637 1.00 106.15 ATOM 5064 NZ LYS 655 56.325 18.246 8.821 1.00 108.43 ATOM 5068 C LYS 655 49.884 16.847 9.935 1.00 93.56 ATOM 5069 O LYS 655 49.904 16.182 10.972 1.00 93.72 ATOM 5070 N LYS 656 49.670 16.320 8.735 1.00 94.19 ATOM 5072 CA LYS 656 49.500 14.886 8.545 1.00 94.84 ATOM 5073 CB LYS 656 48.628 14.620 7.320 1.00 94.64 ATOM 5074 CG LYS 656 47.155 14.874 7.542 1.00 95.54 ATOM 5075 CD LYS 656 46.402 14.709 6.241 1.00 99.56 ATOM 5076 CE LYS 656 44.926 14.449 6.473 1.00 101.77 ATOM 5077 NZ LYS 656 44.202 14.327 5.173 1.00 103.77 ATOM 5081 C LYS 656 50.859 14.225 8.368 1.00 95.18 ATOM 5082 O LYS 656 51.823 14.878 7.956 1.00 95.74 ATOM 5083 N GLY 660 48.651 9.665 5.782 1.00 58.76 ATOM 5085 CA GLY 660 47.932 10.910 6.012 1.00 56.04 ATOM 5086 C GLY 660 47.241 10.937 7.364 1.00 53.90 ATOM 5087 O GLY 660 46.183 11.552 7.525 1.00 53.92 ATOM 5088 N ARG 661 47.838 10.243 8.328 1.00 51.87 ATOM 5090 CA ARG 661 47.297 10.177 9.679 1.00 48.23 ATOM 5091 CB ARG 661 47.755 8.891 10.377 1.00 49.74 ATOM 5092 CG ARG 661 47.506 7.620 9.566 1.00 47.59 ATOM 5093 CD ARG 661 47.561 6.390 10.446 1.00 51.85 ATOM 5094 NE ARG 661 47.584 5.155 9.663 1.00 52.94 ATOM 5096 CZ ARG 661 48.035 3.988 10.117 1.00 52.19 ATOM 5097 NH1 ARG 661 48.503 3.884 11.356 1.00 52.10 ATOM 5100 NH2 ARG 661 48.036 2.926 9.327 1.00 54.43 ATOM 5103 C ARG 661 47.722 11.401 10.483 1.00 43.67 ATOM 5104 O ARG 661 48.658 12.103 10.104 1.00 41.45 ATOM 5105 N LEU 662 47.019 11.656 11.579 1.00 40.27 ATOM 5107 CA LEU 662 47.310 12.799 12.437 1.00 37.15 ATOM 5108 CB LEU 662 46.021 13.533 12.783 1.00 37.39 ATOM 5109 CG LEU 662 45.301 14.149 11.588 1.00 37.67 ATOM 5110 CD1 LEU 662 43.852 14.428 11.937 1.00 35.38 ATOM 5111 CD2 LEU 662 46.041 15.407 11.163 1.00 39.79 ATOM 5112 C LEU 662 47.973 12.330 13.716 1.00 34.68 ATOM 5113 O LEU 662 47.327 11.718 14.568 1.00 33.33 ATOM 5114 N PRO 663 49.260 12.655 13.892 1.00 34.11 ATOM 5115 CD PRO 663 50.086 13.389 12.924 1.00 33.67 ATOM 5116 CA PRO 663 50.052 12.281 15.068 1.00 33.55 ATOM 5117 CB PRO 663 51.367 13.003 14.833 1.00 32.99 ATOM 5118 CG PRO 663 51.479 12.966 13.328 1.00 36.09 ATOM 5119 C PRO 663 49.412 12.665 16.399 1.00 33.55 ATOM 5120 O PRO 663 49.683 12.036 17.426 1.00 34.11 ATOM 5121 N VAL 664 48.566 13.697 16.387 1.00 32.63 ATOM 5123 CA VAL 664 47.874 14.092 17.613 1.00 32.24 ATOM 5124 CB VAL 664 46.953 15.327 17.396 1.00 33.24 ATOM 5125 CG1 VAL 664 47.779 16.583 17.252 1.00 35.01 ATOM 5126 CG2 VAL 654 46.089 15.154 16.155 1.00 35.44 ATOM 5127 C VAL 664 47.072 12.896 18.150 1.00 31.08 ATOM 5128 O VAL 664 46.866 12.760 19.360 1.00 31.4.9 ATOM 5129 N LYS 665 46.710 11.978 17.255 1.00 29.75 ATOM 5131 CA LYS 665 45.956 10.788 17.638 1.00 28.83 ATOM 5132 CB LYS 665 45.411 10.083 16.397 1.00 29.52 ATOM 5133 CG LYS 665 44.242 10.835 15.797 1.00 27.21 ATOM 5134 CD LYS 665 43.905 10.431 14.397 1.00 27.25 ATOM 5135 CE LYS 665 42.684 11.228 13.931 1.00 28.63 ATOM 5136 NZ LYS 665 42.266 10.902 12.545 1.00 25.33 ATOM 5140 C LYS 665 46.718 9.830 18.537 1.00 29.03 ATOM 5141 O LYS 665 46.152 8.869 19.046 1.00 28.37 ATOM 5142 N TRP 666 47.994 10.123 18.765 1.00 30.40 ATOM 5144 CA TRP 666 48.825 9.296 19.628 1.00 31.10 ATOM 5145 CB TRP 666 50.123 8.906 18.917 1.00 29.53 ATOM 5146 CG TRP 666 49.946 7.781 17.966 1.00 27.03 ATOM 5147 CD2 TRP 666 49.407 7.853 16.638 1.00 25.06 ATOM 5148 CE2 TRP 666 49.418 6.546 16.116 1.00 23.83 ATOM 5149 CE3 TRP 666 48.924 8.899 15.835 1.00 26.08 ATOM 5150 CD1 TRP 666 50.257 6.475 18.186 1.00 20.75 ATOM 5151 NE1 TRP 666 49.937 5.729 17.086 1.00 24.92 ATOM 5153 CZ2 TRP 666 48.962 6.245 14.832 1.00 23.95 ATOM 5154 CZ3 TRP 666 48.466 8.604 14.548 1.00 29.09 ATOM 5155 CH2 TRP 666 48.491 7.282 14.060 1.00 29.22 ATOM 5156 C TRP 666 49.174 10.049 20.896 1.00 33.20 ATOM 5157 O TRP 666 49.701 9.469 21.849 1.00 34.39 ATOM 5158 N MET 667 48.862 11.340 20.910 1.00 34.82 ATOM 5160 CA MET 667 49.169 12.175 22.056 1.00 36.31 ATOM 5161 CB MET 667 49.205 13.645 21.651 1.00 40.08 ATOM 5162 CG MET 667 50.475 14.047 20.931 1.00 42.41 ATOM 5163 SD MET 667 50.555 15.818 20.713 1.00 51.31 ATOM 5164 CE MET 667 50.957 15.928 18.949 1.00 45.44 ATOM 5165 C MET 667 48.299 12.003 23.287 1.00 37.81 ATOM 5166 O MET 667 47.081 11.871 23.195 1.00 38.91 ATOM 5167 N ALA 668 48.958 11.964 24.442 1.00 36.47 ATOM 5169 CA ALA 668 48.286 11.846 25.718 1.00 37.06 ATOM 5170 CB ALA 668 49.308 11.654 26.835 1.00 35.76 ATOM 5171 C ALA 668 47.548 13.161 25.893 1.00 38.76 ATOM 5172 O ALA 668 48.000 14.201 25.414 1.00 38.04 ATOM 5173 N PRO 669 46.416 13.142 26.608 1.00 41.60 ATOM 5174 CD PRO 669 45.819 11.981 27.282 1.00 41.64 ATOM 5175 CA PRO 669 45.614 14.347 26.841 1.00 43.25 ATOM 5176 CB PRO 669 44.478 13.827 27.718 1.00 45.08 ATOM 5177 CG PRO 669 44.383 12.368 27.325 1.00 44.04 ATOM 5178 C PRO 669 46.390 15.486 27.526 1.00 44.68 ATOM 5179 O PRO 669 46.304 16.644 27.111 1.00 43.79 ATOM 5180 N GLU 670 47.135 15.164 28.580 1.00 44.29 ATOM 5182 CA GLU 670 47.905 16.195 29.266 1.00 45.36 ATOM 5183 CB GLU 670 48.596 15.637 30.509 1.00 46.97 ATOM 5184 CG GLU 670 49.858 14.819 30.243 1.00 50.04 ATOM 5185 CD GLU 670 49.588 13.345 30.070 1.00 51.35 ATOM 5186 OE1 GLU 670 50.512 12.552 30.327 1.00 50.99 ATOM 5187 OE2 GLU 670 48.458 12.975 29.700 1.00 52.70 ATOM 5188 C GLU 670 48.942 16.802 28.320 1.00 45.63 ATOM 5189 O GLU 670 49.174 18.006 28.340 1.00 44.75 ATOM 5190 N ALA 671 49.546 15.962 27.482 1.00 46.18 ATOM 5192 CA ALA 671 50.555 16.406 26.531 1.00 46.44 ATOM 5193 CB ALA 671 51.218 15.203 25.860 1.00 43.27 ATOM 5194 C ALA 671 49.931 17.313 25.483 1.00 47.85 ATOM 5195 O ALA 671 50.485 18.355 25.150 1.00 47.61 ATOM 5196 N LEU 672 48.748 16.928 25.018 1.00 51.40 ATOM 5198 CA LEU 672 48.010 17.657 23.990 1.00 54.25 ATOM 5199 CE LEU 672 46.996 16.705 23.346 1.00 55.60 ATOM 5200 CG LEU 672 46.202 17.113 22.105 1.00 58.92 ATOM 5201 CD1 LEU 672 47.114 17.425 20.932 1.00 58.60 ATOM 5202 CD2 LEU 672 45.269 15.977 21.753 1.00 60.32 ATOM 5203 C LEU 672 47.315 18.925 24.514 1.00 55.91 ATOM 5204 O LEU 672 47.289 19.958 23.837 1.00 55.72 ATOM 5205 N PHE 673 46.782 18.846 25.730 1.00 57.88 ATOM 5207 CA PHE 673 46.089 19.977 26.342 1.00 60.07 ATOM 5208 CE PHE 673 44.873 19.484 27.127 1.00 57.08 ATOM 5209 CG PHE 673 43.876 18.742 26.290 1.00 56.39 ATOM 5210 CD1 PHE 673 43.191 17.653 26.813 1.00 57.67 ATOM 5211 CD2 PHE 673 43.633 19.116 24.970 1.00 55.36 ATOM 5212 CE1 PHE 673 42.281 16.939 26.036 1.00 57.42 ATOM 5213 CE2 PHE 673 42.724 18.410 24.183 1.00 55.91 ATOM 5214 CZ PHE 673 42.049 17.317 24.720 1.00 56.42 ATOM 5215 C PHE 673 46.974 20.854 27.238 1.00 63.00 ATOM 5216 O PHE 673 46.926 22.085 27.155 1.00 65.31 ATOM 5217 N ASP 674 47.786 20.223 28.081 1.00 64.08 ATOM 5219 CA ASP 674 48.656 20.954 28.999 1.00 64.97 ATOM 5220 CB ASP 674 48.545 20.375 30.409 1.00 65.13 ATOM 5221 CG ASP 674 47.128 20.358 30.923 1.00 67.33 ATOM 5222 OD1 ASP 674 46.684 19.283 31.372 1.00 66.68 ATOM 5223 OD2 ASP 674 46.462 21.416 30.869 1.00 69.20 ATOM 5224 C ASP 674 50.132 20.971 28.603 1.00 66.38 ATOM 5225 O ASP 674 50.984 21.304 29.434 1.00 68.44 ATOM 5226 N ARG 675 50.441 20.585 27.365 1.00 65.68 ATOM 5228 CA ARG 675 51.829 20.550 26.883 1.00 63.71 ATOM 5229 CB ARG 675 52.321 21.970 26.576 1.00 63.67 ATOM 5230 CG ARG 675 51.491 22.685 25.531 1.00 67.65 ATOM 5231 CD ARG 675 52.094 24.034 25.146 1.00 73.20 ATOM 5232 NE ARG 675 53.382 23.911 24.457 1.00 74.09 ATOM 5234 CZ ARG 675 54.159 24.939 24.122 1.00 73.41 ATOM 5235 NH1 ARG 675 53.788 26.182 24.408 1.00 72.90 ATOM 5238 NH2 ARG 675 55.324 24.720 23.524 1.00 71.96 ATOM 5241 C ARG 675 52.780 19.864 27.876 1.00 61.41 ATOM 5242 O ARG 675 53.960 20.208 27.966 1.00 62.62 ATOM 5243 N ILE 676 52.248 18.903 28.627 1.00 59.15 ATOM 5245 CA ILE 676 53.016 18.162 29.623 1.00 56.88 ATOM 5246 CE ILE 676 52.175 17.904 30.891 1.00 56.26 ATOM 5247 CG2 ILE 676 52.871 16.904 31.807 1.00 53.11 ATOM 5248 CG1 ILE 676 51.920 19.224 31.614 1.00 57.86 ATOM 5249 CD1 ILE 676 51.038 19.096 32.835 1.00 61.05 ATOM 5250 C ILE 676 53.494 16.828 29.070 1.00 56.58 ATOM 5251 O ILE 676 52.727 15.869 28.985 1.00 58.12 ATOM 5252 N TYR 677 54.760 16.773 28.680 1.00 54.34 ATOM 5254 CA TYR 677 55.340 15.556 28.143 1.00 51.14 ATOM 5255 CE TYR 677 56.240 15.868 26.954 1.00 52.37 ATOM 5256 CG TYR 677 55.488 16.315 25.719 1.00 56.21 ATOM 5257 CD1 TYR 677 55.187 17.660 25.512 1.00 56.78 ATOM 5258 CE1 TYR 677 54.534 18.086 24.353 1.00 57.54 ATOM 5259 CD2 TYR 677 55.113 15.395 24.738 1.00 57.82 ATOM 5260 CE2 TYR 677 54.458 15.809 23.571 1.00 59.32 ATOM 5261 CZ TYR 677 54.177 17.159 23.385 1.00 59.59 ATOM 5262 OH TYR 677 53.557 17.589 22.230 1.00 60.15 ATOM 5264 C TYR 677 56.124 14.854 29.224 1.00 48.64 ATOM 5265 O TYR 677 57.040 15.430 29.812 1.00 50.45 ATOM 5266 N THR 678 55.733 13.621 29.510 1.00 44.59 ATOM 5268 CA THR 678 56.397 12.834 30.524 1.00 42.21 ATOM 5269 CB THR 678 55.524 12.726 31.791 1.00 43.55 ATOM 5270 OG1 THR 678 54.302 12.045 31.475 1.00 47.42 ATOM 5272 CG2 THR 678 55.190 14.105 32.327 1.00 48.74 ATOM 5273 C THR 678 56.634 11.432 29.992 1.00 39.94 ATOM 5274 O THR 678 56.207 11.085 28.892 1.00 39.34 ATOM 5275 N HIS 679 57.312 10.616 30.784 1.00 38.54 ATOM 5277 CA HIS 679 57.532 9.248 30.390 1.00 38.29 ATOM 5278 CB HIS 679 58.441 8.546 31.391 1.00 39.51 ATOM 5279 CG HIS 679 59.869 8.997 31.331 1.00 43.13 ATOM 5280 CD2 HIS 679 60.630 9.668 32.233 1.00 43.49 ATOM 5281 ND1 HIS 679 60.694 8.726 30.263 1.00 43.00 ATOM 5283 CE1 HIS 679 61.903 9.201 30.510 1.00 43.62 ATOM 5284 NE2 HIS 679 61.889 9.778 31.695 1.00 44.68 ATOM 5286 C HIS 679 56.147 8.599 30.359 1.00 39.42 ATOM 5287 O HIS 6.79 55.898 7.667 29.593 1.00 40.00 ATOM 5288 N GLN 680 55.228 9.156 31.142 1.00 38.96 ATOM 5290 CA GLN 680 53.867 8.649 31.209 1.00 38.84 ATOM 5291 CB GLN 680 53.214 9.010 32.543 1.00 40.90 ATOM 5292 CG GLN 680 53.835 8.278 33.732 1.00 44.42 ATOM 5293 CD GLN 680 53.677 6.756 33.660 1.00 44.47 ATOM 5294 OE1 GLN 680 52.595 6.225 33.908 1.00 45.52 ATOM 5295 NE2 GLN 680 54.767 6.050 33.348 1.00 42.06. ATOM 5298 C GLN 680 53.013 9.099 30.036 1.00 38.25 ATOM 5299 O GLN 680 51.968 8.505 29.758 1.00 39.27 ATOM 5300 N SER 681 53.427 10.155 29.349 1.00 37.00 ATOM 5302 CA SER 681 52.665 10.571 28.182 1.00 38.02 ATOM 5303 CB SER 681 52.929 12.034 27.813 1.00 40.29 ATOM 5304 OG SER 681 54.307 12.286 27.620 1.00 47.29 ATOM 5306 C SER 681 53.066 9.620 27.051 1.00 37.43 ATOM 5307 O SER 681 52.289 9.366 26.136 1.00 37.86 ATOM 5308 N ASP 682 54.281 9.077 27.162 1.00 35.23 ATOM 5310 CA ASP 682 54.800 8.106 26.205 1.00 33.24 ATOM 5311 CB ASP 682 56.284 7.820 26.464 1.00 31.85. ATOM 5312 CG ASP 682 57.224 8.732 25.677 1.00 34.18 ATOM 5313 OD1 ASP 682 58.445 8.537 25.826 1.00 31.79 ATOM 5314 OD2 ASP 682 56.763 9.620 24.908 1.00 29.15 ATOM 5315 C ASP 682 54.015 6.810 26.374 1.00 31.52 ATOM 5316 O ASP 682 53.788 6.087 25.411 1.00 31.93 ATOM 5317 N VAL 683 53.653 6.499 27.617 1.00 33.14 ATOM 5319 CA VAL 683 52.879 5.293 27.935 1.00 32.79 ATOM 5320 CB VAL 683 52.725 5.095 29.478 1.00 34.56 ATOM 5321 CG1 VAL 683 51.653 4.059 29.790 1.00 32.39 ATOM 5322 CG2 VAL 683 54.050 4.649 30.088 1.00 28.08 ATOM 5323 C VAL 683 51.506 5.338 27.245 1.00 31.45 ATOM 5324 O VAL 683 51.008 4.311 26.779 1.00 30.37 ATOM 5325 N TRP 684 50.919 6.531 27.147 1.00 31.04 ATOM 5327 CA TRP 684 49.638 6.686 26.464 1.00 31.23 ATOM 5328 CB TRP 684 49.158 8.137 26.525 1.00 34.14 ATOM 5329 CG TRP 684 47.913 8.423 25.694 1.00 37.17 ATOM 5330 CD2 TRP 684 46.573 8.593 26.187 1.00 38.61 ATOM 5331 CE2 TRP 684 45.755 8.888 25.064 1.00 37.91 ATOM 5332 CE3 TRP 684 45.978 8.528 27.452 1.00 37.63 ATOM 5333 CD1 TRP 684 47.850 8.612 24.337 1.00 37.39 ATOM 5334 NE1 TRP 684 46.560 8.894 23.956 1.00 34.76 ATOM 5336 CZ2 TRP 684 44.380 9.118 25.181 1.00 34.79 ATOM 5337 CZ3 TRP 684 44.611 8.759 27.563 1.00 38.53 ATOM 5338 CH2 TRP 684 43.830 9.048 26.428 1.00 37.59 ATOM 5339 C TRP 684 49.876 6.294 2.5.013 1.00 29.99 ATOM 5340 O TRP 684 49.254 5.356 24.503 1.00 30.82 ATOM 5341 N SER 685 50.815 6.992 24.380 1.00 28.28 ATOM 5343 CA SER 685 51.174 6.738 22.986 1.00 27.54 ATOM 5344 CB SER 685 52.444 7.504 22.631 1.00 26.69 ATOM 5345 OG SER 685 52.355 8.874 22.986 1.00 32.15 ATOM 5347 C SER 685 51.399 5.249 22.737 1.00 26.41 ATOM 5348 O SER 685 50.968 4.709 21.713 1.00 29.52 ATOM 5349 N PHE 686 52.065 4.582 23.676 1.00 26.47 ATOM 5351 CA PHE 686 52.325 3.151 23.563 1.00 26.35 ATOM 5352 CB PHE 686 53.167 2.668 24.754 1.00 25.01 ATOM 5353 CG PHE 686 53.447 1.182 24.742 1.00 27.24 ATOM 5354 CD1 PHE 686 54.187 0.600 23.712 1.00 24.88 ATOM 5355 CD2 PHE 686 52.915 0.351 25.729 1.00 24.99 ATOM 5356 CE1 PHE 686 54.389 −0.783 23.655 1.00 22.77 ATOM 5357 CE2 PHE 686 53.113 −1.036 25.679 1.00 28.39 ATOM 5358 CZ PHE 686 53.853 −1.601 24.631 1.00 22.71 ATOM 5359 C PHE 686 50.997 2.366 23.466 1.00 28.82 ATOM 5360 O PHE 686 50.892 1.398 22.696 1.00 26.41 ATOM 5361 N GLY 687 49.988 2.797 24.229 1.00 29.65 ATOM 5363 CA GLY 687 48.692 2.134 24.194 1.00 29.88 ATOM 5364 C GLY 687 48.099 2.158 22.794 1.00 29.57 ATOM 5365 O GLY 687 47.560 1.165 22.300 1.00 30.38 ATOM 5366 N VAL 688 48.222 3.310 22.147 1.00 29.19 ATOM 5368 CA VAL 688 47.718 3.478 20.795 1.00 25.09 ATOM 5369 CB VAL 688 47.747 4.956 20.359 1.00 22.52 ATOM 5370 CG1 VAL 688 47.106 5.115 18.985 1.00 21.13 ATOM 5371 CG2 VAL 688 47.001 5.810 21.366 1.00 22.50 ATOM 5372 C VAL 688 48.574 2.636 19.865 1.00 23.82 ATOM 5373 O VAL 688 48.080 2.132 18.871 1.00 25.39 ATOM 5374 N LEU 689 49.849 2.463 20.208 1.00 24.46 ATOM 5376 CA LEU 689 50.764 1.655 19.401 1.00 25.68 ATOM 5377 CB LEU 689 52.222 1.893 19.834 1.00 25.93 ATOM 5378 CG LEU 689 53.374 1.307 19.004 1.00 25.01 ATOM 5379 CD1 LEU 689 54.655 2.080 19.257 1.00 25.86 ATOM 5380 CD2 LEU 689 53.593 −0.145 19.318 1.00 24.90 ATOM 5381 C LEU 689 50.374 0.171 19.531 1.00 26.50 ATOM 5382 O LEU 689 50.464 −0.578 18.558 1.00 27.13 ATOM 5383 N LEU 690 49.927 −0.234 20.724 1.00 27.76 ATOM 5385 CA LEU 690 49.481 −1.610 20.980 1.00 28.59 ATOM 5386 CB LEU 690 49.087 −1.800 22.447 1.00 30.38 ATOM 5387 CG LEU 690 50.121 −2.065 23.545 1.00 29.57 ATOM 5388 CD1 LEU 690 49.435 −1.966 24.907 1.00 27.40 ATOM 5389 CD2 LEU 690 50.744 −3.431 23.360 1.00 28.79 ATOM 5390 C LEU 690 48.242 −1.849 20.134 1.00 28.77 ATOM 5391 O LEU 690 48.055 −2.922 19.573 1.00 28.07 ATOM 5392 N TRP 691 47.383 −0.838 20.075 1.00 29.58 ATOM 5394 CA TRP 691 46.166 −0.921 19.275 1.00 30.53 ATOM 5395 CB TRP 69.1 45.327 0.349 19.451 1.00 28.28 ATOM 5396 CG TRP 691 43.985 0.300 18.769 1.00 25.86 ATOM 5397 CD2 TRP 691 43.702 0.689 17.421 1.00 23.99 ATOM 5398 CE2 TRP 691 42.321 0.498 17.215 1.00 25.08 ATOM 5399 CE3 TRP 691 44.487 1.165 16.367 1.00 20.88 ATOM 5400 CD1 TRP 691 42.791 −0.090 19.314 1.00 23.72 ATOM 5401 NE1 TRP 691 41.786 0.031 18.389 1.00 26.15 ATOM 5403 CZ2 TRP 691 41.704 0.788 15.997 1.00 25.07 ATOM 5404 CZ3 TRP 691 43.883 1.448 15.163 1.00 22.80 ATOM 5405 CE2 TRP 691 42.501 1.251 14.982 1.00 24.95 ATOM 5406 C TRP 691 46.566 −1.116 17.811 1.00 30.63 ATOM 5407 O TRP 691 45.943 −1.892 17.093 1.00 33.02 ATOM 5408 N GLU 692 47.625 −0.431 17.386 1.00 31.00 ATOM 5410 CA GLU 692 48.130 −0.545 16.018 1.00 29.00 ATOM 5411 CB GLU 692 49.285 0.426 15.778 1.00 26.55 ATOM 5412 CG GLU 692 48.873 1.876 15.651 1.00 29.90 ATOM 5413 CD GLU 692 50.040 2.781 15.316 1.00 29.83 ATOM 5414 OE1 GLU 692 50.770 3.174 16.247 1.00 32.18 ATOM 5415 OE2 GLU 692 50.227 3.110 14.124 1.00 31.57 ATOM 5416 C GLU 692 48.622 −1.959 15.735 1.00 29.02 ATOM 5417 O GLU 692 48.474 −2.467 14.627 1.00 29.22 ATOM 5418 N ILE 693 49.258 −2.573 16.724 1.00 29.54 ATOM 5420 CA ILE 693 49.766 −3.933 16.555 1.00 31.01 ATOM 5421 CB ILE 693 50.634 −4.360 17.757 1.00 32.36 ATOM 5422 CG2 ILE 693 51.006 −5.845 17.641 1.00 34.39 ATOM 5423 CG1 ILE 693 51.909 −3.506 17.815 1.00 30.30 ATOM 5424 CD1 ILE 693 52.696 −3.693 19.082 1.00 25.66 ATOM 5425 C ILE 693 48.638 −4.939 16.381 1.00 30.63 ATOM 5426 O ILE 693 48.633 −5.738 15.451 1.00 31.10 ATOM 5427 N PHE 694 47.644 −4.858 17.248 1.00 32.60 ATOM 5429 CA PHE 694 46.543 −5.793 17.172 1.00 33.86 ATOM 5430 CE PHE 694 45.938 −5.970 18.563 1.00 35.66 ATOM 5431 CG PHE 694 46.941 −6.499 19.559 1.00 35.70 ATOM 5432 CD1 PHE 694 47.460 −5.684 20.556 1.00 37.18 ATOM 5433 CD2 PHE 694 47.449 −7.794 19.426 1.00 34.37 ATOM 5434 CE1 PHE 694 48.473 −6.150 21.392 1.00 36.90 ATOM 5435 CE2 PHE 694 48.456 −8.265 20.255 1.00 31.89 ATOM 5436 CZ PHE 694 48.970 −7.446 21.234 1.00 34.95 ATOM 5437 C PHE 694 45.532 −5.576 16.049 1.00 34.26 ATOM 5438 O PHE 694 44.702 −6.442 15.787 1.00 37.52 ATOM 5439 N TER 695 45.636 −4.441 15.359 1.00 32.23 ATOM 5441 CA TER 695 44.775 −4.160 14.215 1.00 28.08 ATOM 5442 CB TER 695 44.186 −2.728 14.241 1.00 25.71 ATOM 5443 OG1 TER 695 45.237 −1.762 14.228 1.00 24.94 ATOM 5445 CG2 TER 695 43.353 −2.528 15.468 1.00 23.07 ATOM 5446 C TER 695 45.615 −4.348 12.955 1.00 27.53 ATOM 5447 O TER 695 45.166 −4.066 11.845 1.00 30.89 ATOM 5448 N LEU 696 46.833 −4.848 13.145 1.00 27.73 ATOM 5450 CA LEU 696 47.781 −5.081 12.061 1.00 28.99 ATOM 5451 CB LEU 696 47.370 −6.297 11.226 1.00 27.78 ATOM 5452 CG LEU 696 47.379 −7.591 12.047 1.00 29.89 ATOM 5453 CD1 LEU 696 47.251 −8.823 11.164 1.00 29.96 ATOM 5454 CD2 LEU 696 48.668 −7.656 12.803 1.00 30.20 ATOM 5455 C LEU 696 48.044 −3.853 11.179 1.00 30.33 ATOM 5456 O LEU 696 48.006 −3.926 9.948 1.00 29.41 ATOM 5457 N GLY 697 48.374 −2.738 11.831 1.00 30.92 ATOM 5459 CA GLY 697 48.655 −1.503 11.113 1.00 30.35 ATOM 5460 C GLY 697 47.420 −0.650 10.912 1.00 30.65 ATOM 5461 O GLY 697 47.359 0.178 10.000 1.00 30.01 ATOM 5462 N GLY 698 46.428 −0.836 11.772 1.00 30.50 ATOM 5464 CA GLY 698 45.209 −0.063 11.656 1.00 30.36 ATOM 5465 C GLY 698 45.416 1.415 11.930 1.00 30.07 ATOM 5466 O GLY 698 46.320 1.809 12.666 1.00 30.56 ATOM 5467 N SER 699 44.554 2.228 11.338 1.00 29.65 ATOM 5469 CA SER 699 44.597 3.674 11.485 1.00 28.42 ATOM 5470 CE SER 699 44.263 4.324 10.145 1.00 24.61 ATOM 5471 OG SER 699 43.960 5.693 10.280 1.00 31.25 ATOM 5473 C SER 699 43.621 4.137 12.574 1.00 28.27 ATOM 5474 O SER 699 42.406 3.930 12.474 1.00 27.14 ATOM 5475 N PRO 700 44.160 4.682 13.675 1.00 29.29 ATOM 5476 CD PRO 700 45.587 4.867 13.999 1.00 26.09 ATOM 5477 CA PRO 700 43.303 5.155 14.764 1.00 29.30 ATOM 5478 CE PRO 700 44.319 5.624 15.812 1.00 27.68 ATOM 5479 CG PRO 700 45.531 5.982 14.985 1.00 27.85 ATOM 5480 C PRO 700 42.413 6.305 14.306 1.00 29.71 ATOM 5481 O PRO 700 42.800 7.096 13.446 1.00 31.38 ATOM 5482 N TYR 701 41.204 6.357 14.854 1.00 29.51 ATOM 5484 CA TYR 701 40.246 7.419 14.548 1.00 30.25 ATOM 5485 CB TYR 701 40.559 8.647 15.405 1.00 33.50 ATOM 5486 CG TYR 701 40.321 8.413 16.866 1.00 37.84 ATOM 5487 CD1 TYR 701 41.323 8.638 17.803 1.00 40.05 ATOM 5488 CE1 TYR 701 41.092 8.412 19.158 1.00 42.28 ATOM 5489 CD2 TYR 701 39.084 7.965 17.310 1.00 41.54 ATOM 5490 CE2 TYR 701 38.845 7.738 18.653 1.00 43.70 ATOM 5491 CZ TYR 701 39.845 7.963 19.574 1.00 42.63 ATOM 5492 OH TYR 701 39.584 7.716 20.907 1.00 45.31 ATOM 5494 C TYR 701 40.173 7.829 13.088 1.00 28.45 ATOM 5495 O TYR 701 40.356 9.001 12.760 1.00 29.03 ATOM 5496 N PRO 702 39.901 6.867 12.191 1.00 28.05 ATOM 5497 CD PRO 702 39.671 5.430 12.417 1.00 26.90 ATOM 5498 CA PRO 702 39.815 7.181 10.764 1.00 27.48 ATOM 5499 CB PRO 702 39.610 5.807 10.119 1.00 27.06 ATOM 5500 CG PRO 702 38.923 5.036 11.169 1.00 28.28 ATOM 5501 C PRO 702 38.689 8.145 10.440 1.00 26.81 ATOM 5502 O PRO 702 37.554 7.953 10.865 1.00 26.26 ATOM 5503 N GLY 703 39.035 9.192 9.693 1.00 28.48 ATOM 5505 CA GLY 703 38.085 10.217 9.295 1.00 26.54 ATOM 5506 C GLY 703 37.862 11.285 10.351 1.00 28.03 ATOM 5507 O GLY 703 37.110 12.231 10.108 1.00 28.93 ATOM 5508 N VAL 704 38.518 11.149 11.505 1.00 28.16 ATOM 5510 CA VAL 704 38.369 12.081 12.619 1.00 29.55 ATOM 5511 CB VAL 704 38.473 11.360 13.984 1.00 28.50 ATOM 5512 CG1 VAL 704 38.330 12.350 15.135 1.00 28.07 ATOM 5513 CG2 VAL 704 37.403 10.295 14.091 1.00 29.78 ATOM 5514 C VAL 704 39.375 13.227 12.588 1.00 32.00 ATOM 5515 O VAL 704 40.578 13.028 12.758 1.00 33.85 ATOM 5516 N PRO 705 38.888 14.446 12.336 1.00 33.56 ATOM 5517 CD PRO 705 37.512 14.763 11.906 1.00 33.69 ATOM 5518 CA PRO 705 39.745 15.628 12.280 1.00 32.65 ATOM 5519 CB PRO 705 38.863 16.647 11.569 1.00 34.10 ATOM 5520 CG PRO 705 37.478 16.256 12.021 1.00 36.38 ATOM 5521 C PRO 705 40.164 16.081 13.668 1.00 33.22 ATOM 5522 O PRO 705 39.549 15.708 14.668 1.00 33.26 ATOM 5523 N VAL 706 41.198 16.912 13.710 1.00 34.61 ATOM 5525 CA VAL 706 41.764 17.417 14.954 1.00 37.72 ATOM 5526 CB VAL 706 42.803 18.527 14.673 1.00 39.14 ATOM 5527 CG1 VAL 706 43.483 18.941 15.957 1.00 39.12 ATOM 5528 CG2 VAL 706 43.836 18.038 13.670 1.00 41.07 ATOM 5529 C VAL 706 40.740 17.934 15.969 1.00 38.70 ATOM 5530 O VAL 706 40.761 −17.536 17.136 1.00 38.42 ATOM 5531 N GLU 707 39.834 18.796 15.517 1.00 40.43 ATOM 5533 CA GLU 707 38.823 19.375 16.395 1.00 40.66 ATOM 5534 CB GLU 707 37.973 20.379 15.621 1.00 43.40 ATOM 5535 C GLU 707 37.940 18.316 17.028 1.00 41.03 ATOM 5536 O GLU 707 37.642 18.370 18.231 1.00 41.52 ATOM 5537 N GLU 708 37.560 17.327 16.224 1.00 41.62 ATOM 5539 CA GLU 708 36.708 16.243 16.700 1.00 41.06 ATOM 5540 CB GLU 708 36.179 15.425 15.523 1.00 45.19 ATOM 5541 CG GLU 708 35.281 16.221 14.571 1.00 48.74 ATOM 5542 CD GLU 708 34.063 16.825 15.258 1.00 57.18 ATOM 5543 OE1 GLU 708 33.523 16.203 16.207 1.00 54.30 ATOM 5544 OE2 GLU 708 33.646 17.934 14.837 1.00 61.76 ATOM 5545 C GLU 708 37.443 15.363 17.694 1.00 38.39 ATOM 5546 O GLU 708 36.867 14.927 18.696 1.00 36.76 ATOM 5547 N LEU 709 38.725 15.131 17.434 1.00 37.78 ATOM 5549 CA LEU 709 39.555 14.327 18.324 1.00 38.13 ATOM 5550 CB LEU 709 41.007 14.255 17.820 1.00 35.45 ATOM 5551 CG LEU 709 41.984 13.560 18.786 1.00 35.57 ATOM 5552 CD1 LEU 709 41.825 12.049 18.729 1.00 32.33 ATOM 5553 CD2 LEU 709 43.407 13.965 18.484 1.00 31.98 ATOM 5554 C LEU 709 39.550 14.946 19.716 1.00 38.31 ATOM 5555 O LEU 709 39.362 14.250 20.717 1.00 38.16 ATOM 5556 N PHE 710 39.776 16.254 19.770 1.00 40.09 ATOM 5558 CA PHE 710 39.807 16.973 21.036 1.00 43.6.1 ATOM 5559 CE PHE 710 39.997 18.475 20.797 1.00 48.22 ATOM 5560 CG PHE 710 41.328 18.834 20.192 1.00 51.77 ATOM 5561 CD1 PHE 710 42.395 17.939 20.231 1.00 52.94 ATOM 5562 CD2 PHE 710 41.513 20.072 19.579 1.00 53.99 ATOM 5563 CE1 PHE 710 43.632 18.275 19.679 1.00 56.48 ATOM 5564 CE2 PHE 710 42.746 20.422 19.021 1.00 55.72 ATOM 5565 CZ PHE 710 43.807 19.517 19.069 1.00 57.84 ATOM 5566 C PHE 710 38.519 16.726 21.796 1.00 43.35 ATOM 5567 O PHE 710 38.539 16.424 22.989 1.00 43.22 ATOM 5568 N LYS 711 37.399 16.804 21.083 1.00 44.68 ATOM 5570 CA LYS 711 36.095 16.587 21.690 1.00 43.47 ATOM 5571 CE LYS 711 34.977 16.878 20.687 1.00 44.33 ATOM 5572 C LYS 711 33.601 16.765 21.299 1.00 47.63 ATOM 5573 CD LYS 711 32.510 17.206 20.362 1.00 49.97 ATOM 5574 CE LYS 711 31.158 16.873 20.960 1.00 51.70 ATOM 5575 NZ LYS 711 30.038 17.412 20.150 1.00 57.55 ATOM 5579 C LYS 711 35.986 15.173 22.261 1.00 42.72 ATOM 5580 O LYS 711 35.589 14.999 23.420 1.00 41.16 ATOM 5581 N LEU 712 36.392 14.176 21.471 1.00 42.52 ATOM 5583 CA LEU 712 36.361 12.770 21.898 1.00 42.52 ATOM 5584 CE LEU 712 36.922 11.843 20.809 1.00 41.56 ATOM 5585 CG LEU 712 36.090 11.528 19.560 1.00 41.87 ATOM 5586 CD1 LEU 712 36.902 10.620 18.636 1.00 36.28 ATOM 5587 CD2 LEU 712 34.760 10.868 19.951 1.00 37.19 ATOM 5588 C LEU 712 37.158 12.564 23.180 1.00 42.34 ATOM 5589 O LEU 712 36.697 11.886 24.107 1.00 40.77 ATOM 5590 N LEU 713 38.366 13.121 23.208 1.00 42.68 ATOM 5592 CA LEU 713 39.240 13.025 24.371 1.00 44.05 ATOM 5593 CB LEU 713 40.581 13.710 24.100 1.00 45.45 ATOM 5594 CG LEU 713 41.418 13.114 22.963 1.00 44.78 ATOM 5595 CD1 LEU 713 42.676 13.945 22.750 1.00 41.89 ATOM 5596 CD2 LEU 713 41.757 11.660 23.282 1.00 43.21 ATOM 5597 C LEU 713 38.571 13.654 25.591 1.00 44.66 ATOM 5598 O LEU 713 38.562 13.051 26.662 1.00 45.70 ATOM 5599 N LYS 714 37.980 14.839 25.418 1.00 43.05 ATOM 5601 CA LYS 714 37.300 15.510 26.524 1.00 42.19 ATOM 5602 CB LYS 714 36.884 16.921 26.127 1.00 42.41 ATOM 5603 CG LYS 714 38.076 17.828 25.918 1.00 46.10 ATOM 5604 CD LYS 714 37.684 19.259 25.589 1.00 .49.86 ATOM 5605 CE LYS 714 38.939 20.097 25.292 1.00 52.55 ATOM 5606 NZ LYS 714 39.889 20.148 26.459 1.00 50.17 ATOM 5610 C LYS 714 36.104 14.728 27.054 1.00 42.39 ATOM 5611 O LYS 714 35.767 14.824 28.237 1.00 43.44 ATOM 5612 N GLU 715 35.480 13.934 26.192 1.00 40.44 ATOM 5614 CA GLU 715 34.342 13.118 26.593 1.00 37.90 ATOM 5615 CE GLU 715 33.408 12.893 25.411 1.00 39.54 ATOM 5616 CG GLU 715 32.800 14.174 24.846 1.00 45.20 ATOM 5617 CD GLU 715 32.032 13.936 23.563 1.00 47.85 ATOM 5618 OE1 GLU 715 32.409 13.008 22.810 1.00 50.00 ATOM 5619 OE2 GLU 715 31.061 14.677 23.304 1.00 50.41 ATOM 5620 C GLU 715 34.793 11.773 27.157 1.00 37.31 ATOM 5621 O GLU 715 33.970 10.907 27.450 1.00 36.79 ATOM 5622 N GLY 716 36.102 11.585 27.286 1.00 36.60 ATOM 5624 CA GLY 716 36.623 10.336 27.819 1.00 37.11 ATOM 5625 C GLY 716 36.503 9.140 26.887 1.00 38.30 ATOM 5626 O GLY 716 36.603 7.994 27.340 1.00 36.84 ATOM 5627 N HIS 717 36.307 9.404 25.592 1.00 40.24 ATOM 5629 CA HIS 717 36.167 8.353 24.579 1.00 42.63 ATOM 5630 CB HIS 717 35.800 8.951 23.217 1.00 43.11 ATOM 5631 CG HIS 717 35.745 7.941 22.112 1.00 44.69 ATOM 5632 CD2 HIS 717 34.756 7.101 21.717 1.00 45.13 ATOM 5633 ND1 HIS 717 36.818 7.683 21.283 1.00 47.31 ATOM 5635 CE1 HIS 717 36.494 6.728 20.426 1.00 47.61 ATOM 5636 NE2 HIS 717 35.250 6.357 20.670 1.00 44.95 ATOM 5638 C HIS 717 37.451 7.567 24.413 1.00 44.84 ATOM 5639 O HIS 717 38.528 8.152 24.295 1.00 46.79 ATOM 5640 N ARG 718 37.313 6.247 24.337 1.00 45.44 ATOM 5642 CA ARG 718 38.440 5.345 24.170 1.00 45.36 ATOM 5643 CB ARG 718 38.614 4.496 25.434 1.00 43.82 ATOM 5644 CG ARG 718 38.976 5.308 26.687 1.00 44.52 ATOM 5645 CD ARG 718 40.284 6.065 26.476 1.00 45.02 ATOM 5646 NE ARG 718 40.718 6.856 27.630 1.00 43.12 ATOM 5648 CZ ARG 718 40.550 8.173 27.744 1.00 44.77 ATOM 5649 NH1 ARG 718 39.940 8.859 26.784 1.00 44.67 ATOM 5652 NH2 ARG 718 41.067 8.826 28.777 1.00 46.39 ATOM 5655 C ARG 718 38.124 4.474 22.952 1.00 45.94 ATOM 5656 O ARG 718 36.953 4.243 22.645 1.00 47.59 ATOM 5657 N MET 719 39.145 4.077 22.204 1.00 45.34 ATOM 5659 CA MET 719 38.925 3.253 21.029 1.00 44.28 ATOM 5660 CE MET 719 40.198 3.125 20.185 1.00 42.30 ATOM 5661 CG MET 719 40.575 4.399 19.441 1.00 38.44 ATOM 5662 SD MET 719 42.000 4.225 18.368 1.00 36.97 ATOM 5663 CE MET 719 43.317 4.219 19.511 1.00 36.09 ATOM 5664 C MET 719 38.415 1.877 21.418 1.00 46.21 ATOM 5665 O MET 719 38.708 1.393 22.517 1.00 43.29 ATOM 5666 N ASP 720 37.659 1.267 20.498 1.00 48.79 ATOM 5668 CA ASP 720 37.069 −0.063 20.666 1.00 48.87 ATOM 5669 CE ASP 720 36.099 −0.369 19.513 1.00 54.01 ATOM 5670 CG ASP 720 34.766 0.374 19.632 1.00 59.30 ATOM 5671 OD1 ASP 720 34.762 1.583 19.981 1.00 62.96 ATOM 5672 OD2 ASP 720 33.716 −0.259 19.354 1.00 58.64 ATOM 5673 C ASP 720 38.126 −1.154 20.688 1.00 46.10 ATOM 5674 O ASP 720 39.213 −0.992 20.125 1.00 44.13 ATOM 5675 N LYS 721 37.788 −2.272 21.322 1.00 45.27 ATOM 5677 CA LYS 721 38.689 −3.413 21.404 1.00 43.25 ATOM 5678 CE LYS 721 38.172 −4.436 22.416 1.00 42.02 ATOM 5679 CG LYS 721 39.072 −5.651 22.557 1.00 46.57 ATOM 5680 CD LYS 721 38.602 −6.576 23.666 1.00 49.96 ATOM 5681 CE LYS 721 38.300 −7.971 23.141 1.00 51.80 ATOM 5682 NZ LYS 721 37.937 −8.920 24.240 1.00 56.08 ATOM 5686 C LYS 721 38.769 −4.055 20.031 1.00 43.67 ATOM 5687 O LYS 721 37.736 −4.313 19.394 1.00 44.02 ATOM 5688 N PRO 722 39.995 −4.233 19.513 1.00 43.94 ATOM 5689 CD PRO 722 41.281 −3.711 20.001 1.00 45.90. ATOM 5690 CA PRO 722 40.159 −4.853 18.198 1.00 43.96 ATOM 5691 CE PRO 722 41.665 −4.720 17.941 1.00 43.11 ATOM 5692 CG PRO 722 42.046 −3.509 18.715 1.00 45.16 ATOM 5693 C PRO 722 39.772 −6.317 18.295 1.00 43.09 ATOM 5694 O PRO 722 39.764 −6.888 19.385 1.00 41.32 ATOM 5695 N SER 723 39.382 −6.902 17.170 1.00 45.79 ATOM 5697 CA SER 723 39.044 −8.316 17.144 1.00 46.67 ATOM 5698 CE SER 723 38.303 −8.664 15.857 1.00 44.69 ATOM 5699 OG SER 723 39.131 −8.414 14.736 1.00 49.79 ATOM 5701 C SER 723 40.422 −8.961 17.148 1.00 46.90 ATOM 5702 O SER 723 41.360 −8.411 16.581 1.00 48.81 ATOM 5703 N ASN 724 40.540 −10.131 17.760 1.00 49.28 ATOM 5705 CA ASN 724 41.826 −10.804 17.849 1.00 52.10 ATOM 5706 CE ASN 724 42.480 −10.947 16.469 1.00 55.86 ATOM 5707 CG ASN 724 41.774 −11.957 15.592 1.00 58.72 ATOM 5708 OD2 ASN 724 41.686 −13.140 15.941 1.00 62.28 ATOM 5709 ND2 ASN 724 41.258 −11.503 14.449 1.00 59.56 ATOM 5712 C ASN 724 42.665 −9.931 18.770 1.00 51.97 ATOM 5713 O ASN 724 43.621 −9.274 18.369 1.00 53.85 ATOM 5714 N CYS 725 42.202 −9.859 20.004 1.00 51.02 ATOM 5716 CA CYS 725 42.853 −9.094 21.049 1.00 50.18 ATOM 5717 CB CYS 725 42.708 −7.583 20.811 1.00 47.75 ATOM 5718 SG CYS 725 43.424 −6.577 22.130 1.00 44.37 ATOM 5719 C CYS 725 42.131 −9.507 22.315 1.00 49.31 ATOM 5720 O CYS 725 40.916 −9.371 22.417 1.00 49.90 ATOM 5721 N THR 726 42.866 −10.088 23.249 1.00 48.52 ATOM 5723 CA THR 726 42.262 −10.541 24.490 1.00 49.58 ATOM 5724 CB THR 726 43.251 −11.444 25.291 1.00 49.84 ATOM 5725 OG1 THR 726 44.236 −10.648 25.976 1.00 49.05 ATOM 5727 CG2 THR 726 43.982 −12.363 24.352 1.00 47.96 ATOM 5728 C THR 726 41.788 −9.369 25.356 1.00 49.93 ATOM 5729 O THR 726 42.305 −8.256 25.244 1.00 51.55 ATOM 5730 N ASN 727 40.829 −9.622 26.242 1.00 50.48 ATOM 5732 CA ASN 727 40.335 −8.577 27.144 1.00 52.17 ATOM 5733 CB ASN 727 39.190 −9.099 28.016 1.00 57.57 ATOM 5734 CG ASN 727 39.533 −10.409 28.714 1.00 66.49 ATOM 5735 OD1 ASN 727 40.709 −10.786 28.833 1.00 70.43 ATOM 5736 ND2 ASN 727 38.500 −11.122 29.175 1.00 68.43 ATOM 5739 C ASN 727 41.491 −8.091 28.023 1.00 50.29 ATOM 5740 O ASN 727 41.467 −6.976 28.540 1.00 49.88 ATOM 5741 N GLU 728 42.518 −8.927 28.163 1.00 50.60 ATOM 5743 CA GLU 728 43.700 −8.597 28.956 1.00 49.33 ATOM 5744 CB GLU 728 44.529 −9.859 29.220 1.00 50.44 ATOM 5745 CG GLU 728 45.802 −9.600 30.008 1.00 55.30 ATOM 5746 CD GLU 728 46.577 −10.862 30.354 1.00 57.40 ATOM 5747 OE1 GLU 728 46.716 −11.754 29.489 1.00 5675 ATOM 5748 OE2 GLU 728 47.062 −10.950 31.502 1.00 59.85 ATOM 5749 C GLU 728 44.539 −7.552 28.212 1.00 47.08 ATOM 5750 O GLU 728 44.888 −6.512 28.776 1.00 48.02 ATOM 5751 N LEU 729 44.846 −7.821 26.945 1.00 43.34 ATOM 5753 CA LEU 729 45.630 −6.891 26.129 1.00 42.01 ATOM 5754 CB LEU 729 45.899 −7.500 24.751 1.00 39.46 ATOM 5755 CG LEU 729 46.911 −8.639 24.772 1.00 40.31 ATOM 5756 CD1 LEU 729 46.782 −9.482 23.531 1.00 42.21 ATOM 5757 CD2 LEU 729 48.314 −8.068 24.900 1.00 42.49 ATOM 5758 C LEU 729 44.901 −5.557 25.980 1.00 40.61 ATOM 5759 O LEU 729 45.510 −4.481 25.953 1.00 38.33 ATOM 5760 N TYR 730 43.580 −5.637 25.909 1.00 39.07 ATOM 5762 CA TYR 730 42.761 −4.455 25.773 1.00 38.61 ATOM 5763 CB TYR 730 41.341 −4.837 25.369 1.00 36.79 ATOM 5764 CG TYR 730 40.454 −3.646 25.125 1.00 37.08 ATOM 5765 CD1 TYR 730 40.760 −2.721 24.127 1.00 32.86 ATOM 5766 CE1 TYR 730 39.961 −1.616 23.912 1.00 29.79 ATOM 5767 CD2 TYR 730 39.328 −3.420 25.916 1.00 36.99 ATOM 5768 CE2 TYR 730 38.522 −2.312 25.704 1.00 36.69 ATOM 5769 CZ TYR 730 38.853 −1.412 24.706 1.00 32.69 ATOM 5770 OH TYR 730 38.044 −0.320 24.492 1.00 38.80 ATOM 5772 C TYR 730 42.767 −3.662 27.080 1.00 39.75 ATOM 5773 O TYR 730 42.781 −2.430 27.065 1.00 40.53 ATOM 5774 N MET 731 42.738 −4.360 28.210 1.00 41.88 ATOM 5776 CA MET 731 42.778 −3.684 29.509 1.00 45.34 ATOM 5777 CB MET 731 42.658 −4.697 30.646 1.00 53.46 ATOM 5778 CG MET 731 41.253 −5.248 30.836 1.00 64.30 ATOM 5779 SD MET 731 40.134 −4.095 31.653 1.00 75.78 ATOM 5780 CE MET 731 40.657 −4.338 33.370 1.00 69.70 ATOM 5781 C MET 731 44.099 −2.927 29.614 1.00 41.53 ATOM 5782 O MET 731 44.157 −1.814 30.138 1.00 37.91 ATOM 5783 N MET 732 45.156 −3.545 29.098 1.00 40.48 ATOM 5785 CA MET 732 46.478 −2.937 29.091 1.00 40.23 ATOM 5786 CB MET 732 47.508 −3.872 28.436 1.00 40.29 ATOM 5787 CG MET 732 48.929 −3.307 28.390 1.00 38.07 ATOM 5788 SD MET 732 50.171 −4.522 27.908 1.00 37.65 ATOM 5789 CE MET 732 50.407 −5.343 29.431 1.00 37.90 ATOM 5790 C MET 732 46.378 −1.623 28.317 1.00 38.96 ATOM 5791 O MET 732 46.843 −0.591 28.790 1.00 41.36 ATOM 5792 N MET 733 45.744 −1.663 27.148 1.00 36.94 ATOM 5794 CA MET 733 45.574 −0.463 26.340 1.00 35.19 ATOM 5795 CB MET 733 44.796 −0.769 25.070 1.00 36.07 ATOM 5796 CG MET 733 45.549 −1.577 24.048 1.00 35.99 ATOM 5797 SD MET 733 44.471 −1.851 22.641 1.00 40.05 ATOM 5798 CE MET 733 45.244 −3.351 21.909 1.00 33.13 ATOM 5799 C MET 733 44.800 0.560 27.141 1.00 37.29 ATOM 5800 O MET 733 45.207 1.719 27.245 1.00 39.14 ATOM 5801 N ARG 734 43.690 0.125 27.735 1.00 38.76 ATOM 5803 CA ARG 734 42.849 1.014 28.532 1.00 39.49 ATOM 5804 CB ARG 734 41.577 0.297 28.993 1.00 40.33 ATOM 5805 CG ARG 734 40.699 −0.225 27.856 1.00 38.02 ATOM 5806 CD ARG 734 40.256 0.877 26.909 1.00 42.72 ATOM 5807 NE ARG 734 39.443 1.898 27.567 1.00 48.85 ATOM 5809 CZ ARG 734 38.120 1.838 27.700 1.00 52.35 ATOM 5810 NH1 ARG 734 37.435 0.811 27.222 1.00 54.79 ATOM 5813 NH2 ARG 734 37.477 2.804 28.338 1.00 54.69 ATOM 5816 C ARG 734 43.627 1.587 29.715 1.00 38.70 ATOM 5817 O ARG 734 43.445 2.757 30.068 1.00 40.92 ATOM 5818 N ASP 735 44.530 0.782 30.276 1.00 38.76 ATOM 5820 CA ASP 735 45.379 1.208 31.399 1.00 38.60 ATOM 5821 CB ASP 735 46.325 0.087 31.825 1.00 41.34 ATOM 5822 CG ASP 735 45.622 −1.022 32.574 1.00 44.66 ATOM 5823 OD1 ASP 735 46.048 −2.194 32.428 1.00 43.15 ATOM 5824 OD2 ASP 735 44.657 −0.713 33.313 1.00 44.46 ATOM 5825 C ASP 735 46.215 2.385 30.938 1.00 37.76 ATOM 5826 O ASP 735 46.235 3.446 31.585 1.00 36.35 ATOM 5827 N CYS 736 46.890 2.182 29.805 1.00 35.39 ATOM 5829 CA CYS 736 47.730 3.196 29.181 1.00 34.77 ATOM 5830 CB CYS 736 48.379 2.652 27.916 1.00 30.62 ATOM 5831 SG CYS 736 49.453 1.261 28.198 1.00 30.96 ATOM 5832 C CYS 736 46.938 4.429 28.814 1.00 35.98 ATOM 5833 O CYS 736 47.516 5.491 28.606 1.00 37.38 ATOM 5834 N TRP 737 45.620 4.290 28.713 1.00 38.50 ATOM 5836 CA TRP 737 44.772 5.423 28.370 1.00 40.16 ATOM 5837 CB TRP 737 43.791 5.028 27.271 1.00 38.41 ATOM 5838 CG TRP 737 44.453 4.586 26.011 1.00 39.33 ATOM 5839 CD2 TRP 737 43.893 3.718 25.020 1.00 39.64 ATOM 5840 CE2 TRP 737 44.852 3.583 23.992 1.00 39.97 ATOM 5841 CE3 TRP 737 42.672 3.040 24.900 1.00 37.06 ATOM 5842 CD1 TRP 737 45.695 4.932 25.556 1.00 39.56 ATOM 5843 NE1 TRP 737 45.941 4.336 24.343 1.00 38.61 ATOM 5845 CZ2 TRP 737 44.627 2.795 22.859 1.00 38.78 ATOM 5846 CZ3 TRP 737 42.452 2.261 23.778 1.00 38.90 ATOM 5847 CH2 TRP 737 43.426 2.145 22.772 1.00 38.18 ATOM 5848 C TRP 737 44.028 6.029 29.563 1.00 41.30 ATOM 5849 O TRP 737 42.979 6.658 29.398 1.00 41.45 ATOM 5850 N HIS 738 44.575 5.873 30.763 1.00 43.01 ATOM 5852 CA HIS 738 43.932 6.423 31.948 1.00 44.64 ATOM 5853 CB HIS 738 44.454 5.735 33.205 1.00 46.20 ATOM 5854 CG HIS 738 43.742 6.154 34.458 1.00 50.35 ATOM 5855 CD2 HIS 738 43.473 7.379 34.963 1.00 49.09 ATOM 5856 ND1 HIS 738 43.220 5.244 35.355 1.00 49.94 ATOM 5858 CE1 HIS 738 42.659 5.899 36.357 1.00 52.92 ATOM 5859 NE2 HIS 738 42.798 7.194 36.146 1.00 46.91 ATOM 5861 C HIS 738 44.174 7.921 32.037 1.00 45.26 ATOM 5862 O HIS 738 45.314 8.356 32.021 1.00 45.31 ATOM 5863 N ALA 739 43.099 8.686 32.224 1.00 46.61 ATOM 5865 CA ALA 739 43.155 10.150 32.322 1.00 48.49 ATOM 5866 CE ALA 739 41.823 10.681 32.790 1.00 49.69 ATOM 5867 C ALA 739 44.272 10.682 33.224 1.00 50.77 ATOM 5868 O ALA 739 45.004 11.601 32.846 1.00 51.77 ATOM 5869 N VAL 740 44.336 10.138 34.439 1.00 51.47 ATOM 5871 CA VAL 740 45.352 10.485 35.439 1.00 51.09 ATOM 5872 CE VAL 740 44.897 10.075 36.850 1.00 52.40 ATOM 5873 CG1 VAL 740 45.847 10.624 37.878 1.00 53.38 ATOM 5874 CG2 VAL 740 43.485 10.544 37.105 1.00 55.18 ATOM 5875 C VAL 740 46.649 9.727 35.130 1.00 48.99 ATOM 5876 O VAL 740 46.773 8.534 35.440 1.00 47.72 ATOM 5877 N PRO 741 47.646 10.421 34.565 1.00 48.31 ATOM 5878 CD PRO 741 47.603 11.861 34.253 1.00 47.84 ATOM 5879 CA PRO 741 48.949 9.852 34.197 1.00 48.51 ATOM 5880 CE PRO 741 49.762 11.087 33.828 1.00 46.83 ATOM 5881 CG PRO 741 48.714 12.000 33.255 1.00 46.21 ATOM 5882 C PRO 741 49.641 9.016 35.275 1.00 49.12 ATOM 5883 O PRO 741 50.449 8.139 34.955 1.00 46.57 ATOM 5884 N SER 742 49.327 9.290 36.541 1.00 49.47 ATOM 5886 CA SER 742 49.928 8.557 37.651 1.00 49.50 ATOM 5887 CE SER 742 49.760 9.326 38.963 1.00 51.06 ATOM 5888 OG SER 742 48.403 9.638 39.209 1.00 53.81 ATOM 5890 C SER 742 49.339 7.159 37.787 1.00 48.81 ATOM 5891 O SER 742 49.926 6.284 38.427 1.00 49.45 ATOM 5892 N GLN 743 48.164 6.959 37.203 1.00 47.82 ATOM 5894 CA GLN 743 47.529 5.658 37.273 1.00 46.34 ATOM 5895 CB GLN 743 46.022 5.791 37.432 1.00 49.74 ATOM 5896 CG GLN 743 45.519 5.305 38.784 1.00 55.41 ATOM 5897 CD GLN 743 46.178 6.030 39.947 1.00 59.15 ATOM 5898 OE1 GLN 743 46.905 5.425 40.748 1.00 59.02 ATOM 5899 NE2 GLN 743 45.922 7.338 40.052 1.00 60.03 ATOM 5902 C GLN 743 47.874 4.768 36.095 1.00 44.34 ATOM 5903 O GLN 743 47.548 3.578 36.114 1.00 44.64 ATOM 5904 N ARG 744 48.497 5.339 35.059 1.00 42.83 ATOM 5906 CA ARG 744 48.914 4.559 33.880 1.00 40.34 ATOM 5907 CB ARG 744 49.349 5.469 32.724 1.00 35.84 ATOM 5908 CG ARG 744 48.296 6.406 32.190 1.00 28.25 ATOM 5909 CD ARG 744. 48.906 7.383 31.216 1.00 22.56 ATOM 5910 NE ARG 744 47.948 8.437 30.922 1.00 28.09 ATOM 5912 CZ ARG 744 48.258 9.658 30.493 1.00 32.83 ATOM 5913 NH1 ARG 744 49.524 10.001 30.278 1.00 34.44 ATOM 5916 NH2 ARG 744 47.307 10.569 30.360 1.00 32.00 ATOM 5919 C ARG 744 50.110 3.712 34.295 1.00 41.58 ATOM 5920 O ARG 744 50.906 4.124 35.145 1.00 45.48 ATOM 5921 N PRO 745 50.223 2.489 33.754 1.00 40.97 ATOM 5922 CD PRO 745 49.345 1.749 32.831 1.00 39.90 ATOM 5923 CA PRO 745 51.381 1.685 34.157 1.00 39.77 ATOM 5924 CB PRO 745 51.063 0.311 33.558 1.00 39.31 ATOM 5925 CG PRO 745 50.255 0.642 32.344 1.00 40.98 ATOM 5926 C PRO 745 52.664 2.269 33.573 1.00 38.44 ATOM 5927 O PRO 745 52.631 3.009 32.595 1.00 39.64 ATOM 5928 N THR 746 53.783 2.001 34.224 1.00 37.50 ATOM 5930 CA THR 746 55.066 2.462 33.728 1.00 37.56 ATOM 5931 CB THR 746 56.108 2.571 34.869 1.00 38.58 ATOM 5932 OG1 THR 746 56.286 1.285 35.487 1.00 43.28 ATOM 5934 CG2 THR 746 55.666 3.567 35.899 1.00 34.64 ATOM 5935 C THR 746 55.546 1.393 32.739 1.00 36.49 ATOM 5936 O THR 746 55.118 0.234 32.817 1.00 34.18 ATOM 5937 N PHE 747 56.453 1.768 31.839 1.00 35.27 ATOM 5939 CA PHE 747 56.995 0.814 30.880 1.00 33.48 ATOM 5940 CB PHE 747 58.025 1.475 29.970 1.00 34.35 ATOM 5941 CG PHE 747 57.419 2.369 28.920 1.00 32.49 ATOM 5942 CD1 PHE 747 56.715 1.825 27.856 1.00 30.69 ATOM 5943 CD2 PHE 747 57.519 3.749 29.018 1.00 32.81 ATOM 5944 CB1 PHE 747 56.122 2.639 26.907 1.00 29.41 ATOM 5945 CB2 PHE 747 56.926 4.573 28.072 1.00 32.93 ATOM 5946 CZ PHE 747 56.223 4.014 27.015 1.00 31.50 ATOM 5947 C PHE 747 57.621 −0.363 31.606 1.00 34.65 ATOM 5948 O PHE 747 57.616 −1.474 31.099 1.00 36.34 ATOM 5949 N LYS 748 58.142 −0.128 32.808 1.00 37.75 ATOM 5951 CA LYS 748 58.748 −1.205 33.583 1.00 39.67 ATOM 5952 CB LYS 748 59.382 −0.664 34.873 1.00 43.06 ATOM 5953 CG LYS 748 59.958 −1.757 35.774 1.00 48.96 ATOM 5954 CD LYS 748 60.750 −1.207 36.966 1.00 52.20 ATOM 5955 CB LYS 748 61.183 −2.344 37.907 1.00 53.62 ATOM 5956 NZ LYS 748 62.057 −1.893 39.031 1.00 54.82 ATOM 5960 C LYS 748 57.680 −2.263 33.882 1.00 39.65 ATOM 5961 O LYS 748 57.902 −3.454 33.652 1.00 38.91 ATOM 5962 N GLN 749 56.503 −1.818 34.331 1.00 39.39 ATOM 5964 CA GLN 749 55.402 −2.742 34.623 1.00 40.70 ATOM 5965 CB GLN 749 54.177 −1.991 35.140 1.00 43.82 ATOM 5966 CG GLN 749 54.395 −1.149 36.373 1.00 50.97 ATOM 5967 CD GLN 749 53.175 −0.304 36.715 1.00 55.53 ATOM 5968 OE1 GLN 749 53.272 0.914 36.895 1.00 55.80 ATOM 5969 NE2 GLN 749 52.012 −0.940 36.773 1.00 60.05 ATOM 5972 C GLN 749 55.009 −3.455 33.334 1.00 40.03 ATOM 5973 O GLN 749 54.903 −4.679 33.298 1.00 40.26 ATOM 5974 N LEU 750 54.802 −2.666 32.278 1.00 39.18 ATOM 5976 CA LEU 750 54.400 −3.171 30.964 1.00 36.65 ATOM 5977 CB LEU 750 54.369 −2.039 29.927 1.00 34.58 ATOM 5978 CG LEU 750 53.355 −0.910 30.116 1.00 32.52 ATOM 5979 CD1 LEU 750 53.644 0.210 29.125 1.00 31.67 ATOM 5980 CD2 LEU 750 51.947 −1.435 29.935 1.00 31.37 ATOM 5981 C LEU 750 55.321 −4.255 30.477 1.00 35.81 ATOM 5982 O LEU 750 54.856 −5.267 29.963 1.00 35.81 ATOM 5983 N VAL 751 56.626 −4.035 30.620 1.00 37.38 ATOM 5985 CA VAL 751 57.607 −5.029 30.193 1.00 38.66 ATOM 5986 CB VAL 751 59.077 −4.545 30.411 1.00 35.42 ATOM 5987 CG1 VAL 751 60.075 −5.646 30.041 1.00 29.83 ATOM 5988 CG2 VAL 751 59.342 −3.324 29.559 1.00 29.95 ATOM 5989 C VAL 751 57.337 −6.314 30.974 1.00 41.63 ATOM 5990 O VAL 751 57.312 −7.401 30.396 1.00 42.43 ATOM 5991 N GLU 752 57.051 −6.174 32.267 1.00 43.35 ATOM 5993 CA GLU 752 56.766 −7.329 33.111 1.00 47.39 ATOM 5994 CB GLU 752 56.674 −6.914 34.587 1.00 50.66 ATOM 5995 CG GLU 752 57.950 −6.243 35.101 1.00 54.77 ATOM 5996 CD GLU 752 58.006 −6.101 36.612 1.00 55.14 ATOM 5997 OE1 GLU 752 58.246 −4.972 37.102 1.00 54.14 ATOM 5998 OE2 GLU 752 57.844 −7.131 37.308 1.00 57.73 ATOM 5999 C GLU 752 55.496 −8.068 32.655 1.00 46.00 ATOM 6000 O GLU 752 55.548 −9.261 32.328 1.00 46.25 ATOM 6001 N ASP 753 54.380 −7.346 32.601 1.00 44.35 ATOM 6003 CA ASP 753 53.099 −7.912 32.180 1.00 44.19 ATOM 6004 CB ASP 753 52.059 −6.814 31.985 1.00 46.22 ATOM 6005 CG ASP 753 51.512 −6.279 33.278 1.00 50.48 ATOM 6006 OD1 ASP 753 51.396 −7.062 34.248 1.00 52.15 ATOM 6007 OD2 ASP 753 51.170 −5.069 33.306 1.00 52.20 ATOM 6008 C ASP 753 53.244 −8.608 30.849 1.00 44.54 ATOM 6009 O ASP 753 52.770 −9.724 30.674 1.00 46.03 ATOM 6010 N LEU 754 53.880 −7.918 29.906 1.00 44.43 ATOM 6012 CA LEU 754 54.079 −8.438 28.563 1.00 43.70 ATOM 6013 CB LEU 754 54.570 −7.339 27.618 1.00 43.48 ATOM 6014 CG LEU 754 53.481 −6.350 27.201 1.00 44.67 ATOM 6015 CD1 LEU 754 54.095 −5.218 26.399 1.00 44.51 ATOM 6016 CD2 LEU 754 52.384 −7.069 26.408 1.00 42.07 ATOM 6017 C LEU 754 54.993 −9.642 28.512 1.00 43.14 ATOM 6018 O LEU 754 54.795 −10.536 27.697 1.00 41.32 ATOM 6019 N ASP 755 55.990 −9.671 29.383 1.00 44.74 ATOM 6021 CA ASP 755 56.897 −10.800 29.426 1.00 47.24 ATOM 6022 CB ASP 755 57.942 −10.575 30.517 1.00 51.26 ATOM 6023 CG ASP 755 59.121 −11.518 30.407 1.00 55.39 ATOM 6024 OD1 ASP 755 59.739 −11.793 31.455 1.00 60.61 ATOM 6025 OD2 ASP 755 59.443 −11.970 29.283 1.00 57.16 ATOM 6026 C ASP 755 56.023 −12.005 29.771 1.00 47.67 ATOM 6027 O ASP 755 56.041 −13.032 29.081 1.00 45.99 ATOM 6028 N ARG 756 55.186 −11.816 30.789 1.00 46.72 ATOM 6030 CA ARG 756 54.272 −12.851 31.256 1.00 46.25 ATOM 6031 CB ARG 756 53.519 −12.368 32.499 1.00 46.31 ATOM 6032 CG ARG 756 52.391 −13.287 32.953 1.00 46.99 ATOM 6033 CD ARG 756 51.733 −12.776 34.227 1.00 48.10 ATOM 6034 NE ARG 756 51.320 −11.379 34.118 1.00 53.67 ATOM 6036 CZ ARG 756 50.294 −10.951 33.385 1.00 55.35 ATOM 6037 NH1 ARG 756 49.562 −11.812 32.684 1.00 54.10 ATOM 6040 NX2 ARG 756 50.008 −9.654 33.344 1.00 56.02 ATOM 6043 C ARG 756 53.282 −13.261 30.175 1.00 45.05 ATOM 6044 O ARG 756 53.213 −14.429 29.806 1.00 47.19 ATOM 6045 N ILE 757 52.550 −12.289 29.647 1.00 43.47 ATOM 6047 CA ILE 757 51.552 −12.553 28.617 1.00 43.80 ATOM 6048 CB ILE 757 50.842 −11.241 28.161 1.00 42.02 ATOM 6049 CG2 ILE 757 49.811 −11.536 27.086 1.00 39.63 ATOM 6050 CG1 ILE 757 50.154 −10.578 29.361 1.00 40.00 ATOM 6051 CD1 ILE 757 49.600 −9.212 29.086 1.00 42.68 ATOM 6052 C ILE 757 52.148 −13.296 27.428 1.00 46.03 ATOM 6053 O ILE 757 51.549 −14.250 26.947 1.00 47.78 ATOM 6054 N VAL 758 53.359 −12.925 27.015 1.00 49.03 ATOM 6056 CA VAL 758 54.015 −13.584 25.884 1.00 51.51 ATOM 6057 CB VAL 758 55.412 −12.971 25.556 1.00 50.75 ATOM 6058 CG1 VAL 758 56.105 −13.780 24.470 1.00 50.31 ATOM 6059 CG2 VAL 758 55.269 −11.541 25.081 1.00 52.52 ATOM 6060 C VAL 758 54.209 −15.050 26.212 1.00 54.30 ATOM 6061 O VAL 758 53.991 −15.915 25.369 1.00 54.80 ATOM 6062 N ALA 759 54.617 −15.311 27.450 1.00 57.65 ATOM 6064 CA ALA 759 54.858 −16.667 27.919 1.00 60.62 ATOM 6065 CB ALA 759 55.423 −16.637 29.327 1.00 60.32 ATOM 6066 C ALA 759 53.571 −17.478 27.889 1.00 63.25 ATOM 6067 O ALA 759 53.568 −18.638 27.478 1.00 65.81 ATOM 6068 N LEU 760 52.475 −16.856 28.305 1.00 63.56 ATOM 6070 CA LEU 760 51.191 −17.533 28.333 1.00 64.25 ATOM 6071 CB LEU 760 50.302 −16.912 29.407 1.00 65.66 ATOM 6072 CG LEU 760 50.894 −16.962 30.820 1.00 65.62 ATOM 6073 CD1 LEU 760 49.988 −16.246 31.809 1.00 64.75 ATOM 6074 CD2 LEU 760 51.109 −18.410 31.227 1.00 66.65 ATOM 6075 C LEU 760 50.483 −17.535 26.984 1.00 64.89 ATOM 6076 O LEU 760 49.390 −18.088 26.860 1.00 66.37 ATOM 6077 N THR 761 51.103 −16.933 25.973 1.00 65.24 ATOM 6079 CA THR 761 50.516 −16.882 24.634 1.00 64.44 ATOM 6080 CB THR 761 50.829 −15.539 23.925 1.00 62.95 ATOM 6081 OG1 THR 761 50.247 −14.463 24.669 1.00 62.70 ATOM 6083 CG2 THR 761 50.249 −15.525 22.521 1.00 60.59 ATOM 6084 C TER 761 51.003 −18.044 23.769 1.00 64.71 ATOM 6085 O THR 761 52.202 −18.201 23.533 1.00 64.70 ATOM 6086 SG CYS 1603 18.536 −8.818 20.295 0.50 33.97 PRT2 ATOM 6087 CG MET 534 69.178 12.159 22.968 0.50 31.30 PRT2 ATOM 6088 SD MET 534 68.892 13.138 24.442 0.50 33.06 PRT2 ATOM 6089 CB MET 534 70.060 12.456 25.568 0.50 34.22 PRT2 ATOM 6090 SG CYS 603 56.041 −7.885 16.319 0.50 37.82 PRT2 ATOM 2682 OH2 TIP3 1 71.788 25.340 2.479 1.00 24.18 ATOM 2685 OH2 TIP3 2 40.022 4.089 16.127 1.00 43.09 ATOM 2688 OH2 TIP3 3 83.745 19.577 10.510 1.00 27.38 ATOM 2691 OH2 TIP3 4 83.420 20.163 7.482 1.00 30.85 ATOM 2694 OH2 TIP3 5 75.022 16.439 6.505 1.00 33.15 ATOM 2697 OH2 TIP3 6 86.308 19.567 9.284 1.00 33.55 ATOM 2700 OH2 TIP3 7 51.888 11.346 24.141 1.00 34.30 ATOM 2703 OH2 TIP3 8 55.125 9.616 22.499 1.00 21.44 ATOM 2706 OH2 TIP3 9 57.087 4.825 32.412 1.00 28.79 ATOM 2709 OH2 TIP3 10 52.142 4.824 13.180 1.00 21.14 ATOM 2712 OH2 TIP3 11 41.312 5.600 22.910 1.00 49.23 ATOM 2715 OH2 TIP3 12 45.083 9.130 21.671 1.00 37.09 ATOM 2718 OH2 TIP3 13 64.608 −2.335 28.803 1.00 44.31 ATOM 2721 OH2 TIP3 14 77.192 13.199 23.753 1.00 32.96 ATOM 2724 OH2 TIP3 15 79.201 17.296 17.997 1.00 38.51 ATOM 2727 OH2 TIP3 16 82.988 11.608 15.745 1.00 27.56 ATOM 2730 OH2 TIP3 17 14.096 −9.819 0.333 1.00 23.53 ATOM 2733 OH2 TIP3 18 38.325 0.249 5.313 1.00 43.17 ATOM 2736 OH2 TIP3 19 26.939 6.001 5.100 1.00 30.00 ATOM 2739 OH2 TIP3 20 34.305 −1.615 16.992 1.00 44.82 ATOM 2742 OH2 TIP3 21 20.300 2.328 27.798 1.00 45.23 ATOM 2745 OH2 TIP3 22 50.996 −11.607 38.052 1.00 43.49 ATOM 2748 OH2 TIP3 23 17.261 −6.167 −1.444 1.00 27.13 ATOM 2751 OH2 TIP3 24 27.724 8.124 14.996 1.00 31.20 ATOM 2754 OH2 TIP3 25 31.558 0.294 6.872 1.00 34.54 ATOM 2757 OH2 TIP3 26 26.907 −12.815 28.161 1.00 49.20 ATOM 2760 OH2 TIP3 27 28.705 −17.192 13.269 1.00 30.16 ATOM 2763 OH2 TIP3 28 88.639 13.953 7.692 1.00 41.04 ATOM 2766 OH2 TIP3 29 −2.328 −3.576 11.086 1.00 44.89 ATOM 2769 OH2 TIP3 30 34.919 −4.069 19.070 1.00 53.72 ATOM 2772 OH2 TIP3 31 80.124 17.865 9.324 1.00 28.96 ATOM 2775 OH2 TIP3 32 5.417 3.492 10.771 1.00 34.07 ATOM 2778 OH2 TIP3 33 −10.718 4.889 11.542 1.00 30.81 ATOM 2781 OH2 TIP3 34 29.486 −8.823 20.599 1.00 51.35 ATOM 2784 OH2 TIP3 35 6.151 3.065 13.821 1.00 34.56 ATOM 2787 OH2 TIP3 36 31.907 2.919 0.361 1.00 48.13 ATOM 2790 OH2 TIP3 37 19.974 1.928 −3.873 1.00 30.12 ATOM 2793 OH2 TIP3 38 61.976 2.660 32.604 1.00 36.01 ATOM 2796 OH2 TIP3 39 21.084 −7.119 −3.759 1.00 20.12 ATOM 2799 OH2 TIP3 40 −15.729 8.693 22.468 1.00 54.88 ATOM 2802 OH2 TIP3 41 40.160 2.461 8.734 1.00 37.95 ATOM 2805 OH2 TIP3 42 19.248 11.349 0.190 1.00 37.63 ATOM 2808 OH2 TIP3 43 66.856 9.143 17.185 1.00 27.91 ATOM 2811 OH2 TIP3 44 87.262 19.150 18.734 1.00 57.83 ATOM 2814 OH2 TIP3 45 74.597 17.144 3.987 1.00 42.19 ATOM 2817 OH2 TIP3 46 29.192 16.988 10.582 1.00 37.28 ATOM 2820 OH2 TIP3 47 66.415 7.073 14.829 1.00 34.86 ATOM 2823 OH2 TIP3 48 85.063 21.453 5.510 1.00 27.42 ATOM 2826 OH2 TIP3 49 −4.716 2.835 2.998 1.00 40.54 ATOM 2829 OH2 TIP3 50 19.369 5.069 4.888 1.00 38.40 ATOM 2832 OH2 TIP3 51 34.750 5.517 24.999 1.00 29.11 ATOM 2835 OH2 TIP3 52 34.740 −16.765 14.093 1.00 32.68 ATOM 2838 OH2 TIP3 53 59.994 7.555 27.844 1.00 32.60 ATOM 2842 OH2 TIP3 54 −7.401 −1.595 6.080 1.00 43.73 ATOM 2844 OH2 TIP3 55 55.257 12.084 25.108 1.00 44.32 ATOM 2847 OH2 TIP3 56 68.239 6.953 16.647 1.00 44.46 ATOM 2850 OH2 TIP3 57 73.621 20.852 18.820 1.00 29.47 ATOM 2853 OH2 TIP3 58 3.399 −8.294 −8.210 1.00 22.31 ATOM 2856 OH2 TIP3 59 37.999 10.824 5.505 1.00 31.62 ATOM 2859 OH2 TIP3 60 29.779 −9.515 −1.395 1.00 40.76 ATOM 2862 OH2 TIP3 61 49.114 1.432 12.261 1.00 29.92 ATOM 2865 OH2 TIP3 62 41.257 4.012 29.005 1.00 39.24 ATOM 2868 OH2 TIP3 63 11.113 −12.848 1.296 1.00 34.36 ATOM 2871 OH2 TIP3 64 −1.221 −4.593 21.504 1.00 34.24 ATOM 2874 OH2 TIP3 65 30.002 16.453 13.258 1.00 49.66 ATOM 2877 OH2 TIP3 66 8.212 4.106 3.434 1.00 36.54 ATOM 2880 OH2 TIP3 67 72.868 18.807 22.589 1.00 38.26 ATOM 2883 OH2 TIP3 68 −8.056 −3.666 25.021 1.00 39.81 ATOM 2886 OH2 TIP3 69 66.436 −4.683 28.008 1.00 60.97 ATOM 2889 OH2 TIP3 70 22.063 −20.641 4.804 1.00 42.25 ATOM 2892 OH2 TIP3 71 59.860 −7.407 4.859 1.00 56.78 ATOM 2895 OH2 TIP3 72 16.887 −13.832 −2.611 1.00 59.32 ATOM 2898 OH2 TIP3 73 −15.108 7.351 4.303 1.00 31.87 ATOM 2901 OH2 TIP3 74 32.901 2.922 13.663 1.00 37.89 ATOM 2904 OH2 TIP3 75 0.173 −2.666 11.035 1.00 39.12 ATOM 2907 OH2 TIP3 76 17.533 2.317 5.808 1.00 18.66 ATOM 2910 OH2 TIP3 77 27.183 3.730 6.349 1.00 29.04 ATOM 2913 OH2 TIP3 78 −8.812 5.887 9.703 1.00 30.53 ATOM 2916 OH2 TIP3 79 1.614 −2.195 8.694 1.00 30.79 ATOM 2919 OH2 TIP3 80 −5.304 −3.157 6.846 1.00 47.38 ATOM 2922 OH2 TIP3 81 17.401 2.918 1.973 1.00 20.47 ATOM 2925 OH2 TIP3 82 20.333 3.188 3.159 1.00 24.44 ATOM 2928 OH2 TIP3 83 0.408 −2.516 22.276 1.00 31.11 ATOM 2931 OH2 TIP3 84 20.095 −6.123 −1.372 1.00 17.62 ATOM 2934 OH2 TIP3 85 11.018 −15.627 7.421 1.00 60.29 ATOM 2937 OH2 TIP3 86 4.089 −12.037 11.797 1.00 39.47 ATOM 2940 OH2 TIP3 87 6.459 0.908 −3.278 1.00 30.31 ATOM 2943 OH2 TIP3 88 −13.493 1.004 5.319 1.00 41.13 ATOM 2946 OH2 TIP3 89 15.418 −7.532 0.022 1.00 21.29 ATOM 2949 OH2 TIP3 90 −2.128 −5.834 4.052 1.00 57.55 ATOM 2952 OH2 TIP3 91 12.731 4.833 −4.212 1.00 44.52 ATOM 2955 OH2 TIP3 92 69.320 27.812 2.191 1.00 37.47 ATOM 2958 OH2 TIP3 93 24.851 −12.871 0.285 1.00 44.73 ATOM 2961 OH2 TIP3 94 60.301 −4.459 33.927 1.00 40.13 ATOM 2964 OH2 TIP3 95 10.488 5.951 3.205 1.00 41.53 ATOM 2967 OH2 TIP3 96 −9.708 −4.233 4.439 1.00 29.77 ATOM 2970 OH2 TIP3 97 72.950 −1.768 10.144 1.00 39.69 ATOM 2973 OH2 TIP3 98 −3.287 5.612 30.618 1.00 34.65 ATOM 2976 OH2 TIP3 99 36.658 1.007 11.717 1.00 35.43 ATOM 2979 OH2 TIP3 100 21.221 6.459 16.863 1.00 20.70 ATOM 2982 OH2 TIP3 101 5.833 −8.726 22.274 1.00 47.13 ATOM 2985 OH2 TIP3 102 −13.529 7.868 17.445 1.00 31.95 ATOM 2988 OH2 TIP3 103 26.795 −10.682 −0.807 1.00 28.65 ATOM 2991 OH2 TIP3 104 23.711 1.909 18.309 1.00 28.29 ATOM 2994 OH2 TIP3 105 −2.187 12.232 3.920 1.00 44.98 ATOM 2997 OH2 TIP3 106 59.483 12.398 33.535 1.00 39.58 ATOM 3000 OH2 TIP3 107 4.439 −10.915 1.996 1.00 43.77 ATOM 3003 OH2 TIP3 108 8.041 2.687 0.648 1.00 45.32 ATOM 3006 OH2 TIP3 109 75.836 1.477 25.476 1.00 41.65 ATOM 3009 OH2 TIP3 110 48.604 15.594 14.349 1.00 36.36 ATOM 3012 OH2 TIP3 111 2.396 −11.387 9.259 1.00 34.21 ATOM 3015 OH2 TIP3 112 82.927 26.453 12.807 1.00 36.54 ATOM 3018 OH2 TIP3 113 8.983 −6.631 −3.299 1.00 47.01 ATOM 3021 OH2 TIP3 114 −8.690 4.367 4.504 1.00 41.25 ATOM 3024 OH2 TIP3 115 7.941 −13.921 8.777 1.00 36.12 ATOM 3027 OH2 TIP3 116 51.295 6.440 10.632 1.00 28.37 ATOM 3030 OH2 TIP3 117 20.432 3.771 15.637 1.00 31.22 ATOM 3033 OH2 TIP3 118 72.882 3.887 20.227 1.00 30.22 ATOM 3036 OH2 TIP3 119 5.187 −11.863 22.711 1.00 47.49 ATOM 3039 OH2 TIP3 120 33.889 2.571 16.293 1.00 40.04 ATOM 3042 OH2 TIP3 121 9.504 −12.183 7.160 1.00 31.48 ATOM 3045 OH2 TIP3 122 8.397 3.827 −1.647 1.00 46.92 ATOM 3048 OH2 TIP3 123 7.281 7.321 2.391 1.00 62.46 ATOM 3051 OH2 TIP3 124 35.682 −1.725 0.534 1.00 36.75 ATOM 3054 OH2 TIP3 125 44.465 10.095 11.089 1.00 44.72 ATOM 3057 OH2 TIP3 126 45.247 11.893 21.405 1.00 33.51 ATOM 3060 OH2 TIP3 127 57.386 −10.506 14.020 1.00 45.72 ATOM 3063 OH2 TIP3 128 −3.033 15.103 16.644 1.00 38.48 ATOM 3066 OH2 TIP3 129 85.621 11.111 8.814 1.00 38.13 ATOM 3069 OH2 TIP3 130 13.040 −2.760 2.176 1.00 31.26 ATOM 3072 OH2 TIP3 131 75.607 3.932 20.836 1.00 55.09 ATOM 3075 OH2 TIP3 132 13.080 7.467 −2.358 1.00 35.05 ATOM 3078 OH2 TIP3 133 11.308 −9.967 0.995 1.00 28.96 ATOM 3081 OH2 TIP3 134 13.716 −16.170 3.848 1.00 44.64 ATOM 3084 OH2 TIP3 135 −6.498 −3.706 16.178 1.00 43.17 ATOM 3087 OH2 TIP3 136 25.841 −12.949 3.950 1.00 41.14 ATOM 3090 OH2 TIP3 137 −16.285 10.803 6.585 1.00 45.75 ATOM 3093 OH2 TIP3 138 86.457 12.585 6.477 1.00 36.37 ATOM 3096 OH2 TIP3 139 32.097 −4.644 2.224 1.00 28.35 ATOM 3099 OH2 TIP3 140 44.936 7.528 11.961 1.00 46.60 ATOM 3102 OH2 TIP3 141 80.781 12.162 16.353 1.00 41.46 ATOM 3105 OH2 TIP3 142 2.547 −7.532 −1.453 1.00 41.42 ATOM 3108 OH2 TIP3 143 31.850 −5.907 21.194 1.00 54.70 ATOM 3111 OH2 TIP3 144 74.524 −2.663 12.264 1.00 40.35 ATOM 3114 OH2 TIP3 145 7.592 6.769 −0.931 1.00 58.34 ATOM 3117 OH2 TIP3 146 71.168 5.735 21.648 1.00 27.86 ATOM 3120 OH2 TIP3 147 67.876 −4.900 8.725 1.00 33.58 ATOM 3123 OH2 TIP3 148 0.554 −10.181 6.605 1.00 75.65 ATOM 3126 OH2 TIP3 149 67.965 18.266 10.874 1.00 30.42 ATOM 3129 OH2 TIP3 150 3.509 8.125 4.021 1.00 40.77 ATOM 3132 OH2 TIP3 151 52.216 12.175 18.131 1.00 47.63 ATOM 3135 OH2 TIP3 152 −10.336 6.394 5.014 1.00 48.53 ATOM 3138 OH2 TIP3 153 76.427 1.384 −1.196 1.00 47.21 ATOM 3141 OH2 TIP3 154 10.116 −12.199 17.089 1.00 70.16 ATOM 3144 OH2 TIP3 155 34.043 14.595 18.314 1.00 40.56 ATOM 3147 OH2 TIP3 156 2.488 −8.304 16.835 1.00 64.47 ATOM 3150 OH2 TIP3 157 29.610 1.954 6.685 1.00 48.74 ATOM 3153 OH2 TIP3 158 32.578 −17.270 12.109 1.00 37.35 ATOM 3156 OH2 TIP3 159 42.013 18.106 11.196 1.00 68.33 ATOM 3159 OH2 TIP3 160 87.646 10.346 5.465 1.00 75.39 ATOM 3162 OH2 TIP3 161 69.931 −3.739 24.921 1.00 70.42 ATOM 3165 OH2 TIP3 162 77.277 5.700 23.531 1.00 53.26 ATOM 3168 OH2 TIP3 163 34.172 15.704 1.865 1.00 44.88 ATOM 3171 OH2 TIP3 164 −9.871 7.514 7.751 1.00 39.18 ATOM 3174 OH2 TIP3 165 11.814 5.604 7.443 1.00 46.70 ATOM 3177 OH2 TIP3 166 −8.801 13.912 13.532 1.00 52.89 ATOM 3180 OH2 TIP3 167 32.195 3.409 18.336 1.00 32.33 ATOM 3183 OH2 TIP3 168 −8.858 9.696 24.279 1.00 38.90 ATOM 3186 OH2 TIP3 169 −1.135 −6.924 15.691 1.00 43.05 ATOM 3189 OH2 TIP3 170 79.806 0.323 15.371 1.00 36.91 ATOM 3192 OH2 TIP3 171 67.181 20.622 −1.545 1.00 44.72 ATOM 3195 OH2 TIP3 172 −0.823 3.732 1.065 1.00 52.11 ATOM 3198 OH2 TIP3 173 −0.130 6.021 2.491 1.00 40.87 ATOM 3201 OH2 TIP3 174 −1.027 8.941 1.064 1.00 60.72 ATOM 3204 OH2 TIP3 175 −5.566 8.867 2.163 1.00 47.25 ATOM 3207 OH2 TIP3 176 −7.259 10.294 4.033 1.00 53.61 ATOM 3210 OH2 TIP3 177 2.664 7.247 1.058 1.00 46.41 ATOM 3213 OH2 TIP3 178 5.295 10.728 8.257 1.00 39.84 ATOM 3216 OH2 TIP3 179 63.743 12.726 22.713 1.00 49.55 ATOM 3219 OH2 TIP3 180 79.165 1.016 17.948 1.00 51.41 ATOM 3222 OH2 TIP3 181 13.823 −1.538 −3.942 1.00 39.85 ATOM 3225 OH2 TIP3 182 59.255 3.213 32.873 1.00 76.77 ATOM 3228 OH2 TIP3 183 32.210 13.612 20.027 1.00 60.41 ATOM 3231 OH2 TIP3 184 72.606 16.267 22.574 1.00 60.78 ATOM 3234 OH2 TIP3 185 −0.147 5.713 30.877 1.00 50.19 ATOM 3237 OH2 TIP3 186 −1.207 −4.507 27.969 1.00 65.19 ATOM 3240 OH2 TIP3 187 81.340 15.584 16.808 1.00 64.48 ATOM 3243 OH2 TIP3 188 −17.535 3.884 23.785 1.00 57.17 ATOM 3246 OH2 TIP3 189 27.503 10.697 14.669 1.00 36.11 ATOM 3249 OH2 TIP3 190 34.585 4.535 27.618 1.00 61.68 ATOM 3252 OH2 TIP3 191 −3.701 −4.982 9.069 1.00 43.66 ATOM 3255 OH2 TIP3 192 42.524 7.811 22.390 1.00 34.53 ATOM 3258 OH2 TIP3 193 52.937 11.764 21.790 1.00 36.19 ATOM 3261 OH2 TIP3 194 −7.665 8.600 6.358 1.00 59.08 ATOM 3264 OH2 TIP3 195 86.880 5.187 16.579 1.00 55.88 ATOM 3267 OH2 TIP3 196 55.377 16.147 20.540 1.00 48.25 ATOM 3270 OH2 TIP3 197 51.394 19.664 22.988 1.00 46.81 ATOM 3273 OH2 TIP3 198 20.021 7.087 7.226 1.00 52.98 ATOM 3276 OH2 TIP3 199 28.959 1.819 −3.219 1.00 40.50 ATOM 3279 OH2 TIP3 200 26.533 2.812 −4.295 1.00 54.24 ATOM 3282 OH2 TIP3 201 36.739 3.003 18.397 1.00 42.13 ATOM 3285 OH2 TIP3 202 16.968 −20.752 14.318 1.00 54.54 ATOM 3288 OH2 TIP3 203 28.177 −14.418 6.134 1.00 61.36 ATOM 3291 OH2 TIP3 204 31.488 1.501 −1.796 1.00 47.49 ATOM 3294 OH2 TIP3 205 10.665 −16.494 15.731 1.00 41.42 ATOM 3297 OH2 TIP3 206 6.916 −12.200 6.160 1.00 61.94 ATOM 3300 OH2 TIP3 207 −12.659 14.357 10.908 1.00 52.96 ATOM 3303 OH2 TIP3 208 11.274 9.662 −1.588 1.00 48.45 ATOM 3306 OH2 TIP3 209 11.491 12.484 −1.531 1.00 44.51 ATOM 3309 OH2 TIP3 210 34.037 13.520 −1.011 1.00 48.43 ATOM 3312 OH2 TIP3 211 31.162 18.259 7.980 1.00 44.86 ATOM 3315 OH2 TIP3 212 36.937 11.633 −1.971 1.00 49.85 ATOM 3318 OH2 TIP3 213 64.024 13.599 26.505 1.00 37.53 ATOM 3321 OH2 TIP3 214 36.528 5.933 14.857 1.00 57.04 ATOM 3324 OH2 TIP3 215 90.599 4.042 6.342 1.00 54.08 ATOM 3327 OH2 TIP3 216 50.139 −11.645 10.526 1.00 54.64 ATOM 3330 OH2 TIP3 217 66.523 −1.024 30.536 1.00 39.41 ATOM 3333 OH2 TIP3 218 74.880 18.976 20.591 1.00 41.84 ATOM 3336 OH2 TIP3 219 −3.095 9.744 3.142 1.00 52.35 ATOM 3339 OH2 TIP3 220 5.601 −3.682 25.022 1.00 29.30 ATOM 3342 OH2 TIP3 221 35.616 6.407 12.455 1.00 44.48 ATOM 3345 OH2 TIP3 222 −5.381 16.006 14.081 1.00 44.23 ATOM 3348 OH2 TIP3 223 46.509 −11.503 26.814 1.00 53.82 ATOM 3351 OH2 TIP3 224 −3.791 −5.481 20.929 1.00 61.42 ATOM 3354 OH2 TIP3 225 1.622 −3.876 −0.402 1.00 58.60 ATOM 3357 OH2 TIP3 226 86.244 11.220 23.133 1.00 59.84 ATOM 3360 OH2 TIP3 227 11.011 7.959 5.659 1.00 63.07 ATOM 3363 OH2 TIP3 228 64.610 −8.031 20.406 1.00 48.11 ATOM 3366 OH2 TIP3 229 11.446 −17.829 13.438 1.00 51.35 ATOM 3369 OH2 TIP3 230 72.056 1.258 −1.830 1.00 43.88 ATOM 3372 OH2 TIP3 231 57.359 9.732 11.744 1.00 65.45 ATOM 3375 OH2 TIP3 232 43.344 20.728 30.066 1.00 61.52 ATOM 3378 OH2 TIP3 233 66.723 16.772 15.661 1.00 43.79 ATOM 3381 OH2 TIP3 234 88.036 22.036 4.257 1.00 61.83 ATOM 3384 OH2 TIP3 235 12.085 2.346 27.862 1.00 46.29 ATOM 3387 OH2 TIP3 236 64.898 −0.425 3.209 1.00 50.06 ATOM 3390 OH2 TIP3 237 72.114 28.348 7.731 1.00 53.01 ATOM 3393 OH2 TIP3 238 25.792 −8.081 27.181 1.00 55.19 ATOM 3396 OH2 TIP3 239 −18.262 10.614 12.607 1.00 51.54 ATOM 3399 OH2 TIP3 240 30.336 11.280 16.201 1.00 46.53 ATOM 3402 OH2 TIP3 241 22.712 −15.818 −2.226 1.00 47.29 ATOM 3405 OH2 TIP3 242 29.700 9.496 18.074 1.00 40.10 ATOM 3408 OH2 TIP3 243 63.297 −0.480 5.497 1.00 49.90 ATOM 3411 OH2 TIP3 244 61.458 7.093 11.497 1.00 45.71 ATOM 3414 OH2 TIP3 245 −0.217 2.232 32.172 1.00 46.12 ATOM 3417 OH2 TIP3 246 66.196 6.250 12.159 1.00 34.47

[0131] The following abbreviations are used in Tables 3 and 4:

[0132] “Atom Type” refers to the element whose coordinates are provided. The first letter in the column defines the element.

[0133] “A.A.” refers to amino acid.

[0134] “X. Y and Z” provide the Cartesian coordinates of the element.

[0135] “B” is a thermal factor that measures movement of the atom around its atomic center.

[0136] “OCC” refers to occupancy, and represents the percentage of time the atom type occupies the particular coordinate. OCC values range from 0 to 1, with 1 being 100%.

[0137] “PRT1” or “PRT2” relate to occupancy, with PRT1 designating the coordinates of the atom when in the first conformation and PRT2 designating the coordinates of the atom when in the second or alternate conformation.

[0138] Structures coordinates for FLGK according to Tables 3 and 4 may be modified by mathematical manipulation. Such manipulations include, but are not limited to, crystallographic permutations of the raw structure coordinates, fractionalization of the raw structure coordinates, integer additions or subtractions to sets of the raw structure coordinates, inversion of the raw structure coordinates and any combination of the above.

[0139] The present invention is not to be limited in scope by the exemplified embodiments, which are intended as illustrations of single aspects of the invention. Indeed, various modifications of the invention in addition to those described herein will become apparent to those having skill in the art from the foregoing description and accompanying drawings. Such modifications are intended to fall with in the scope of the appended claims.

References

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1 41 1 310 PRT Homo sapiens 1 Met Leu Ala Gly Val Ser Glu Tyr Glu Leu Pro Glu Asp Pro Arg Trp 1 5 10 15 Glu Leu Pro Arg Asp Arg Leu Val Leu Gly Lys Pro Leu Gly Glu Gly 20 25 30 Cys Phe Gly Gln Val Val Leu Ala Glu Ala Ile Gly Leu Asp Lys Asp 35 40 45 Lys Pro Asn Arg Val Thr Lys Val Ala Val Lys Met Leu Lys Ser Asp 50 55 60 Ala Thr Glu Lys Asp Leu Ser Asp Leu Ile Ser Glu Met Glu Met Met 65 70 75 80 Lys Met Ile Gly Lys His Lys Asn Ile Ile Asn Leu Leu Gly Ala Cys 85 90 95 Thr Gln Asp Gly Pro Leu Tyr Val Ile Val Glu Tyr Ala Ser Lys Gly 100 105 110 Asn Leu Arg Glu Tyr Leu Gln Ala Arg Arg Pro Pro Gly Leu Glu Tyr 115 120 125 Cys Tyr Asn Pro Ser His Asn Pro Glu Glu Gln Leu Ser Ser Lys Asp 130 135 140 Leu Val Ser Cys Ala Tyr Gln Val Ala Arg Gly Met Glu Tyr Leu Ala 145 150 155 160 Ser Lys Lys Cys Ile His Arg Asp Leu Ala Ala Arg Asn Val Leu Val 165 170 175 Thr Glu Asp Asn Val Met Lys Ile Ala Asp Phe Gly Leu Ala Arg Asp 180 185 190 Ile His His Ile Asp Tyr Tyr Lys Lys Thr Thr Asn Gly Arg Leu Pro 195 200 205 Val Lys Trp Met Ala Pro Glu Ala Leu Phe Asp Arg Ile Tyr Thr His 210 215 220 Gln Ser Asp Val Trp Ser Phe Gly Val Leu Leu Trp Glu Ile Phe Thr 225 230 235 240 Leu Gly Gly Ser Pro Tyr Pro Gly Val Pro Val Glu Glu Leu Phe Lys 245 250 255 Leu Leu Lys Glu Gly His Arg Met Asp Lys Pro Ser Asn Cys Thr Asn 260 265 270 Glu Leu Tyr Met Met Met Arg Asp Cys Trp His Ala Val Pro Ser Gln 275 280 285 Arg Pro Thr Phe Lys Gln Leu Val Glu Asp Leu Asp Arg Ile Val Ala 290 295 300 Leu Thr Ser Asn Gln Glu 305 310 2 315 PRT Homo sapiens 2 Ser Ala Ala Gly Thr Met Val Ala Gly Val Ser Glu Tyr Glu Leu Pro 1 5 10 15 Glu Asp Pro Arg Trp Glu Leu Pro Arg Asp Arg Leu Val Leu Gly Lys 20 25 30 Pro Leu Gly Glu Gly Ala Phe Gly Gln Val Val Leu Ala Glu Ala Ile 35 40 45 Gly Leu Asp Lys Asp Lys Pro Asn Arg Val Thr Lys Val Ala Val Lys 50 55 60 Met Leu Lys Ser Asp Ala Thr Glu Lys Asp Leu Ser Asp Leu Ile Ser 65 70 75 80 Glu Met Glu Met Met Lys Met Ile Gly Lys His Lys Asn Ile Ile Asn 85 90 95 Leu Leu Gly Ala Cys Thr Gln Asp Gly Pro Leu Tyr Val Ile Val Glu 100 105 110 Tyr Ala Ser Lys Gly Asn Leu Arg Glu Tyr Leu Gln Ala Arg Arg Pro 115 120 125 Pro Gly Leu Glu Tyr Ser Tyr Asn Pro Ser His Asn Pro Glu Glu Gln 130 135 140 Leu Ser Ser Lys Asp Leu Val Ser Cys Ala Tyr Gln Val Ala Arg Gly 145 150 155 160 Met Glu Tyr Leu Ala Ser Lys Lys Cys Ile His Arg Asp Leu Ala Ala 165 170 175 Arg Asn Val Leu Val Thr Glu Asp Asn Val Met Lys Ile Ala Asp Phe 180 185 190 Gly Leu Ala Arg Asp Ile His His Ile Asp Tyr Tyr Lys Lys Thr Thr 195 200 205 Asn Gly Arg Leu Pro Val Lys Trp Met Ala Pro Glu Ala Leu Phe Asp 210 215 220 Arg Ile Tyr Thr His Gln Ser Asp Val Trp Ser Phe Gly Val Leu Leu 225 230 235 240 Trp Glu Ile Phe Thr Leu Gly Gly Ser Pro Tyr Pro Gly Val Pro Val 245 250 255 Glu Glu Leu Phe Lys Leu Leu Lys Glu Gly His Arg Met Asp Lys Pro 260 265 270 Ser Asn Cys Thr Asn Glu Leu Tyr Met Met Met Arg Asp Cys Trp His 275 280 285 Ala Val Pro Ser Gln Arg Pro Thr Phe Lys Gln Leu Val Glu Asp Leu 290 295 300 Asp Arg Ile Val Ala Leu Thr Ser Asn Gln Glu 305 310 315 3 351 PRT Artificial Sequence Description of Artificial Sequence Synthetic protein encoded by recombinant baculovirus 3 Met Arg Gly Ser His His His His His His Gly Met Ala Ser Met Thr 1 5 10 15 Gly Gly Gln Gln Met Gly Arg Asp Leu Tyr Asp Asp Asp Asp Lys Asp 20 25 30 Pro Ser Ser Arg Ser Ala Ala Gly Thr Met Val Ala Gly Val Ser Glu 35 40 45 Tyr Glu Leu Pro Glu Asp Pro Arg Trp Glu Leu Pro Arg Asp Arg Leu 50 55 60 Val Leu Gly Lys Pro Leu Gly Glu Gly Ala Phe Gly Gln Val Val Leu 65 70 75 80 Ala Glu Ala Ile Gly Leu Asp Lys Asp Lys Pro Asn Arg Val Thr Lys 85 90 95 Val Ala Val Lys Met Leu Lys Ser Asp Ala Thr Glu Lys Asp Leu Ser 100 105 110 Asp Leu Ile Ser Glu Met Glu Met Met Lys Met Ile Gly Lys His Lys 115 120 125 Asn Ile Ile Asn Leu Leu Gly Ala Cys Thr Gln Asp Gly Pro Leu Tyr 130 135 140 Val Ile Val Glu Tyr Ala Ser Lys Gly Asn Leu Arg Glu Tyr Leu Gln 145 150 155 160 Ala Arg Arg Pro Pro Gly Leu Glu Tyr Ser Tyr Asn Pro Ser His Asn 165 170 175 Pro Glu Glu Gln Leu Ser Ser Lys Asp Leu Val Ser Cys Ala Tyr Gln 180 185 190 Val Ala Arg Gly Met Glu Tyr Leu Ala Ser Lys Lys Cys Ile His Arg 195 200 205 Asp Leu Ala Ala Arg Asn Val Leu Val Thr Glu Asp Asn Val Met Lys 210 215 220 Ile Ala Asp Phe Gly Leu Ala Arg Asp Ile His His Ile Asp Tyr Tyr 225 230 235 240 Lys Lys Thr Thr Asn Gly Arg Leu Pro Val Lys Trp Met Ala Pro Glu 245 250 255 Ala Leu Phe Asp Arg Ile Tyr Thr His Gln Ser Asp Val Trp Ser Phe 260 265 270 Gly Val Leu Leu Trp Glu Ile Phe Thr Leu Gly Gly Ser Pro Tyr Pro 275 280 285 Gly Val Pro Val Glu Glu Leu Phe Lys Leu Leu Lys Glu Gly His Arg 290 295 300 Met Asp Lys Pro Ser Asn Cys Thr Asn Glu Leu Tyr Met Met Met Arg 305 310 315 320 Asp Cys Trp His Ala Val Pro Ser Gln Arg Pro Thr Phe Lys Gln Leu 325 330 335 Val Glu Asp Leu Asp Arg Ile Val Ala Leu Thr Ser Asn Gln Glu 340 345 350 4 933 DNA Homo sapiens 4 atgctagcag gggtctctga gtatgagctt cccgaagacc ctcgctggga gctgcctcgg 60 gacagactgg tcttaggcaa acccctggga gagggctgct ttgggcaggt ggtgttggca 120 gaggctatcg ggctggacaa ggacaaaccc aaccgtgtga ccaaagtggc tgtgaagatg 180 ttgaagtcgg acgcaacaga gaaagacttg tcagacctga tctcagaaat ggagatgatg 240 aagatgatcg ggaagcataa gaatatcatc aacctgctgg gggcctgcac gcaggatggt 300 cccttgtatg tcatcgtgga gtatgcctcc aagggcaacc tgcgggagta cctgcaggcc 360 cggaggcccc cagggctgga atactgctac aaccccagcc acaacccaga ggagcagctc 420 tcctccaagg acctggtgtc ctgcgcctac caggtggccc gaggcatgga gtatctggcc 480 tccaagaagt gcatacaccg agacctggca gccaggaatg tcctggtgac agaggacaat 540 gtgatgaaga tagcagactt tggcctcgca cgggacattc accacatcga ctactataaa 600 aagacaacca acggccgact gcctgtgaag tggatggcac ccgaggcatt atttgaccgg 660 atctacaccc accagagtga tgtgtggtct ttcggggtgc tcctgtggga gatcttcact 720 ctgggcggct ccccataccc cggtgtgcct gtggaggaac ttttcaagct gctgaaggag 780 ggtcaccgca tggacaagcc cagtaactgc accaacgagc tgtacatgat gatgcgggac 840 tgctggcatg cagtgccctc acagagaccc accttcaagc agctggtgga agacctggac 900 cgcatcgtgg ccttgacctc caaccaggag tag 933 5 1056 DNA Homo sapiens 5 atgcggggtt ctcatcatca tcatcatcat ggtatggcta gcatgactgg tggacagcaa 60 atgggtcggg atctgtacga cgatgacgat aaggatccga gctcgagatc tgcagctggt 120 accatggtag caggggtctc tgagtatgag cttcccgaag accctcgctg ggagctgcct 180 cgggacagac tggtcttagg caaacccctg ggagagggcg cctttgggca ggtggtgttg 240 gcagaggcta tcgggctgga caaggacaaa cccaaccgtg tgaccaaagt ggctgtgaag 300 atgttgaagt cggacgcaac agagaaagac ttgtcagacc tgatctcaga aatggagatg 360 atgaagatga tcgggaagca taagaatatc atcaacctgc tgggggcctg cacgcaggat 420 ggtcccttgt atgtcatcgt ggagtatgcc tccaagggca acctgcggga gtacctgcag 480 gcccggaggc ccccagggct ggaatactcc tacaacccca gccacaaccc agaggagcag 540 ctctcctcca aggacctggt gtcctgcgcc taccaggtgg cccgaggcat ggagtatctg 600 gcctccaaga agtgcataca ccgagacctg gcagccagga atgtcctggt gacagaggac 660 aatgtgatga agatagcaga ctttggcctc gcacgggaca ttcaccacat cgactactat 720 aaaaagacaa ccaacggccg actgcctgtg aagtggatgg cacccgaggc attatttgac 780 cggatctaca cccaccagag tgatgtgtgg tctttcgggg tgctcctgtg ggagatcttc 840 actctgggcg gctccccata ccccggtgtg cctgtggagg aacttttcaa gctgctgaag 900 gagggtcacc gcatggacaa gcccagtaac tgcaccaacg agctgtacat gatgatgcgg 960 gactgctggc atgcagtgcc ctcacagaga cccaccttca agcagctggt ggaagacctg 1020 gaccgcatcg tggccttgac ctccaaccag gagtag 1056 6 310 PRT Homo sapiens 6 Met Leu Ala Gly Val Ser Glu Tyr Glu Leu Pro Glu Asp Pro Arg Trp 1 5 10 15 Glu Leu Pro Arg Asp Arg Leu Val Leu Gly Lys Pro Leu Gly Glu Gly 20 25 30 Cys Phe Gly Gln Val Val Leu Ala Glu Ala Ile Gly Leu Asp Lys Asp 35 40 45 Lys Pro Asn Arg Val Thr Lys Val Ala Val Lys Met Leu Lys Ser Asp 50 55 60 Ala Thr Glu Lys Asp Leu Ser Asp Leu Ile Ser Glu Met Glu Met Met 65 70 75 80 Lys Met Ile Gly Lys His Lys Asn Ile Ile Asn Leu Leu Gly Ala Cys 85 90 95 Thr Gln Asp Gly Pro Leu Tyr Val Ile Val Glu Tyr Ala Ser Lys Gly 100 105 110 Asn Leu Arg Glu Tyr Leu Gln Ala Arg Arg Pro Pro Gly Leu Glu Tyr 115 120 125 Cys Tyr Asn Pro Ser His Asn Pro Glu Glu Gln Leu Ser Ser Lys Asp 130 135 140 Leu Val Ser Cys Ala Tyr Gln Val Ala Arg Gly Met Glu Tyr Leu Ala 145 150 155 160 Ser Lys Lys Cys Ile His Arg Asp Leu Ala Ala Arg Asn Val Leu Val 165 170 175 Thr Glu Asp Asn Val Met Lys Ile Ala Asp Phe Gly Leu Ala Arg Asp 180 185 190 Ile His His Ile Asp Tyr Tyr Lys Lys Thr Thr Asn Gly Arg Leu Pro 195 200 205 Val Lys Trp Met Ala Pro Glu Ala Leu Phe Asp Arg Ile Tyr Thr His 210 215 220 Gln Ser Asp Val Trp Ser Phe Gly Val Leu Leu Trp Glu Ile Phe Thr 225 230 235 240 Leu Gly Gly Ser Pro Tyr Pro Gly Val Pro Val Glu Glu Leu Phe Lys 245 250 255 Leu Leu Lys Glu Gly His Arg Met Asp Lys Pro Ser Asn Cys Thr Asn 260 265 270 Glu Leu Tyr Met Met Met Arg Asp Cys Trp His Ala Val Pro Ser Gln 275 280 285 Arg Pro Thr Phe Lys Gln Leu Val Glu Asp Leu Asp Arg Ile Val Ala 290 295 300 Leu Thr Ser Asn Gln Glu 305 310 7 310 PRT Homo sapiens 7 Met Leu Ala Gly Val Ser Glu Tyr Glu Leu Pro Glu Asp Pro Lys Trp 1 5 10 15 Glu Phe Pro Arg Asp Lys Leu Thr Leu Gly Lys Pro Leu Gly Glu Gly 20 25 30 Cys Phe Gly Gln Val Val Met Ala Glu Ala Val Gly Ile Asp Lys Asp 35 40 45 Lys Pro Lys Glu Ala Val Thr Val Ala Val Lys Met Leu Lys Asp Asp 50 55 60 Ala Thr Glu Lys Asp Leu Ser Asp Leu Val Ser Glu Met Glu Met Met 65 70 75 80 Lys Met Ile Gly Lys His Lys Asn Ile Ile Asn Leu Leu Gly Ala Cys 85 90 95 Thr Gln Asp Gly Pro Leu Tyr Val Ile Val Glu Tyr Ala Ser Lys Gly 100 105 110 Asn Leu Arg Glu Tyr Leu Arg Ala Arg Arg Pro Pro Gly Met Glu Tyr 115 120 125 Ser Tyr Asp Ile Asn Arg Val Pro Glu Glu Gln Met Thr Phe Lys Asp 130 135 140 Leu Val Ser Cys Thr Tyr Gln Leu Ala Arg Gly Met Glu Tyr Leu Ala 145 150 155 160 Ser Gln Lys Cys Ile His Arg Asp Leu Ala Ala Arg Asn Val Leu Val 165 170 175 Thr Glu Asn Asn Val Met Lys Ile Ala Asp Phe Gly Leu Ala Arg Asp 180 185 190 Ile Asn Asn Ile Asp Tyr Tyr Lys Lys Thr Thr Asn Gly Arg Leu Pro 195 200 205 Val Lys Trp Met Ala Pro Glu Ala Leu Phe Asp Arg Val Tyr Thr His 210 215 220 Gln Ser Asp Val Trp Ser Phe Gly Val Leu Met Trp Glu Ile Phe Thr 225 230 235 240 Leu Gly Gly Ser Pro Tyr Pro Gly Ile Pro Val Glu Glu Leu Phe Lys 245 250 255 Leu Leu Lys Glu Gly His Arg Met Asp Lys Pro Ala Asn Cys Thr Asn 260 265 270 Glu Leu Tyr Met Met Met Arg Asp Cys Trp His Ala Val Pro Ser Gln 275 280 285 Arg Pro Thr Phe Lys Gln Leu Val Glu Asp Leu Asp Arg Ile Val Ala 290 295 300 Leu Thr Ser Asn Gln Glu 305 310 8 310 PRT Homo sapiens 8 Met Leu Ala Asn Val Ser Glu Leu Glu Leu Pro Ala Asp Pro Lys Trp 1 5 10 15 Glu Leu Ser Arg Ala Arg Leu Thr Leu Gly Lys Pro Leu Gly Glu Gly 20 25 30 Cys Phe Gly Gln Val Val Met Ala Glu Ala Ile Gly Ile Asp Lys Asp 35 40 45 Arg Ala Ala Lys Pro Val Thr Val Ala Val Lys Met Leu Lys Asp Asp 50 55 60 Ala Thr Asp Lys Asp Leu Ser Asp Leu Val Ser Glu Met Glu Met Met 65 70 75 80 Lys Met Ile Gly Lys His Lys Asn Ile Ile Asn Leu Leu Gly Ala Cys 85 90 95 Thr Gln Gly Gly Pro Leu Tyr Val Leu Val Glu Tyr Ala Ala Lys Gly 100 105 110 Asn Leu Arg Glu Phe Leu Arg Ala Arg Arg Pro Pro Gly Leu Asp Tyr 115 120 125 Ser Phe Asp Thr Cys Lys Pro Pro Glu Glu Gln Leu Thr Phe Lys Asp 130 135 140 Leu Val Ser Cys Ala Tyr Gln Val Ala Arg Gly Met Glu Tyr Leu Ala 145 150 155 160 Ser Gln Lys Cys Ile His Arg Asp Leu Ala Ala Arg Asn Val Leu Val 165 170 175 Thr Glu Asp Asn Val Met Lys Ile Ala Asp Phe Gly Leu Ala Arg Asp 180 185 190 Val His Asn Leu Asp Tyr Tyr Lys Lys Thr Thr Asn Gly Arg Leu Pro 195 200 205 Val Lys Trp Met Ala Pro Glu Ala Leu Phe Asp Arg Val Tyr Thr His 210 215 220 Gln Ser Asp Val Trp Ser Phe Gly Val Leu Leu Trp Glu Ile Phe Thr 225 230 235 240 Leu Gly Gly Ser Pro Tyr Pro Gly Ile Pro Val Glu Glu Leu Phe Lys 245 250 255 Leu Leu Lys Glu Gly His Arg Met Asp Lys Pro Ala Asn Cys Thr His 260 265 270 Asp Leu Tyr Met Ile Met Arg Glu Cys Trp His Ala Ala Pro Ser Gln 275 280 285 Arg Pro Thr Phe Lys Gln Leu Val Glu Asp Leu Asp Arg Val Leu Thr 290 295 300 Val Thr Ser Thr Asp Glu 305 310 9 309 PRT Homo sapiens 9 Leu Leu Ala Gly Leu Val Ser Leu Asp Leu Pro Leu Asp Pro Leu Trp 1 5 10 15 Glu Phe Pro Arg Asp Arg Leu Val Leu Gly Lys Pro Leu Gly Glu Gly 20 25 30 Cys Phe Gly Gln Val Val Arg Ala Glu Ala Phe Gly Met Asp Pro Ala 35 40 45 Arg Pro Asp Gln Ala Ser Thr Val Ala Val Lys Met Leu Lys Asp Asn 50 55 60 Ala Ser Asp Lys Asp Leu Ala Asp Leu Val Ser Glu Met Glu Val Met 65 70 75 80 Lys Leu Ile Gly Arg His Lys Asn Ile Ile Asn Leu Leu Gly Val Cys 85 90 95 Thr Gln Glu Gly Pro Leu Tyr Val Ile Val Glu Cys Ala Ala Lys Gly 100 105 110 Asn Leu Arg Glu Phe Leu Arg Ala Arg Arg Pro Pro Gly Pro Asp Leu 115 120 125 Ser Pro Asp Gly Pro Arg Ser Ser Glu Gly Pro Leu Ser Phe Pro Val 130 135 140 Leu Val Ser Cys Ala Tyr Gln Val Ala Arg Gly Met Gln Tyr Leu Glu 145 150 155 160 Ser Arg Lys Cys Ile His Arg Asp Leu Ala Ala Arg Asn Val Leu Val 165 170 175 Thr Glu Asp Asn Val Met Lys Ile Ala Asp Phe Gly Leu Ala Arg Gly 180 185 190 Val His His Ile Asp Tyr Tyr Lys Lys Thr Ser Asn Gly Arg Leu Pro 195 200 205 Val Lys Trp Met Ala Pro Glu Ala Leu Phe Asp Arg Val Tyr Thr His 210 215 220 Gln Ser Asp Val Trp Ser Phe Gly Ile Leu Leu Trp Glu Ile Phe Thr 225 230 235 240 Leu Gly Gly Ser Pro Tyr Pro Gly Ile Pro Val Glu Glu Leu Phe Ser 245 250 255 Leu Leu Arg Glu Gly His Arg Met Asp Arg Pro Pro His Cys Pro Pro 260 265 270 Glu Leu Tyr Gly Leu Met Arg Glu Cys Trp His Ala Ala Pro Ser Gln 275 280 285 Arg Pro Thr Phe Lys Gln Leu Val Glu Ala Leu Asp Lys Val Leu Leu 290 295 300 Ala Val Ser Glu Glu 305 10 318 PRT Drosophila melanogaster 10 Pro Ala Gln Gly Phe Asn Glu Tyr Glu Phe Pro Leu Asp Ser Asn Trp 1 5 10 15 Glu Ile Pro Arg Gln Gln Leu Ser Leu Gly Ser Ile Leu Gly Glu Gly 20 25 30 Ala Phe Gly Arg Val Val Met Ala Glu Ala Glu Gly Leu Pro Arg Ser 35 40 45 Pro Gln Leu Ala Glu Thr Ile Val Ala Val Lys Met Val Lys Glu Glu 50 55 60 His Thr Asp Thr Asp Met Ala Ser Leu Val Arg Glu Met Glu Val Met 65 70 75 80 Lys Met Ile Gly Lys His Ile Asn Ile Ile Asn Leu Leu Gly Cys Cys 85 90 95 Ser Gln Gly Gly Pro Leu Trp Val Ile Val Glu Tyr Ala Pro His Gly 100 105 110 Asn Leu Lys Asp Phe Leu Lys Gln Asn Arg Pro Gly Ala Pro Gln Arg 115 120 125 Arg Ser Asp Ser Asp Gly Tyr Leu Asp Asp Lys Pro Leu Ile Ser Thr 130 135 140 Gln His Leu Gly Glu Lys Glu Leu Thr Lys Phe Ala Phe Gln Ile Ala 145 150 155 160 Arg Gly Met Glu Tyr Leu Ala Ser Arg Arg Cys Ile His Arg Asp Leu 165 170 175 Ala Ala Arg Asn Val Leu Val Ser Asp Gly Tyr Val Met Lys Ile Ala 180 185 190 Asp Phe Gly Leu Ala Arg Asp Ile Gln Asp Thr Glu Tyr Tyr Arg Lys 195 200 205 Asn Thr Asn Gly Arg Leu Pro Ile Lys Trp Met Ala Pro Glu Ser Leu 210 215 220 Gln Glu Lys Lys Tyr Asp Ser Gln Ser Asp Val Trp Ser Tyr Gly Val 225 230 235 240 Leu Leu Trp Glu Ile Met Thr Tyr Gly Asp Gln Pro Tyr Pro His Ile 245 250 255 Leu Ser Ala Glu Glu Leu Tyr Ser Tyr Leu Ile Thr Gly Gln Arg Met 260 265 270 Glu Lys Pro Ala Lys Cys Ser Leu Asn Ile Tyr Val Val Met Arg Gln 275 280 285 Cys Trp His Phe Gln Ser Cys Ala Arg Pro Thr Phe Ala Glu Leu Val 290 295 300 Glu Ser Phe Asp Gly Ile Leu Gln Gln Ala Ser Ser Asn Pro 305 310 315 11 322 PRT Caenorhabditis elegans 11 Glu Asn Thr Val Leu Ser Glu Tyr Glu Val Asp Ser Asp Pro Val Trp 1 5 10 15 Glu Val Glu Arg Ser Lys Leu Ser Leu Val His Met Leu Gly Glu Gly 20 25 30 Ala Phe Gly Glu Val Trp Lys Ala Thr Tyr Lys Glu Thr Glu Asn Asn 35 40 45 Glu Ile Ala Val Ala Val Lys Lys Leu Lys Met Ser Ala His Glu Lys 50 55 60 Glu Leu Ile Asp Leu Val Ser Glu Met Glu Thr Phe Lys Val Ile Gly 65 70 75 80 Glu His Glu Asn Val Leu Arg Leu Ile Gly Cys Cys Thr Gly Ala Gly 85 90 95 Pro Leu Tyr Val Val Val Glu Leu Cys Lys His Gly Asn Leu Arg Asp 100 105 110 Phe Leu Arg Ala His Arg Pro Lys Glu Glu Lys Ala Lys Lys Ser Ser 115 120 125 Gln Glu Leu Thr Asp Tyr Leu Glu Pro Arg Lys Ala Ser Asp Lys Asp 130 135 140 Asp Ile Glu Leu Ile Pro Asn Leu Thr Gln Arg His Leu Val Gln Phe 145 150 155 160 Ala Trp Gln Val Ala Gln Gly Met Asn Phe Leu Ala Ser Lys Lys Ile 165 170 175 Ile His Arg Asp Leu Ala Ala Arg Asn Val Leu Val Gly Asp Gly His 180 185 190 Val Leu Lys Ile Ser Asp Phe Gly Leu Ser Arg Asp Val His Cys Asn 195 200 205 Asp Tyr Tyr Arg Lys Arg Gly Asn Gly Arg Leu Pro Ile Lys Trp Met 210 215 220 Ala Leu Glu Ala Leu Asp Ser Asn Val Tyr Thr Val Glu Ser Asp Val 225 230 235 240 Trp Ser Tyr Gly Val Leu Leu Trp Glu Ile Met Thr Leu Gly Gly Thr 245 250 255 Pro Tyr Pro Thr Ile Ala Met Pro Glu Leu Tyr Ala Asn Leu Lys Glu 260 265 270 Gly Tyr Arg Met Glu Pro Pro His Leu Cys Pro Gln Glu Val Tyr His 275 280 285 Leu Met Cys Ser Cys Trp Arg Glu Lys Leu Glu Glu Arg Pro Ser Phe 290 295 300 Lys Thr Ile Val Asp Tyr Leu Asp Trp Met Leu Thr Met Thr Asn Glu 305 310 315 320 Thr Ile 12 306 PRT Unknown Organism Description of Unknown Organism Insulin receptor tyrosine kinase 12 Val Phe Pro Cys Ser Val Tyr Val Pro Asp Glu Trp Glu Val Ser Arg 1 5 10 15 Glu Lys Ile Thr Leu Leu Arg Glu Leu Gly Gln Gly Ser Phe Gly Met 20 25 30 Val Tyr Glu Gly Asn Ala Arg Asp Ile Ile Lys Gly Glu Ala Glu Thr 35 40 45 Arg Val Ala Val Lys Thr Val Asn Glu Ser Ala Ser Leu Arg Glu Arg 50 55 60 Ile Glu Phe Leu Asn Glu Ala Ser Val Met Lys Gly Phe Thr Cys His 65 70 75 80 His Val Val Arg Leu Leu Gly Val Val Ser Lys Gly Gln Pro Thr Leu 85 90 95 Val Val Met Glu Leu Met Ala His Gly Asp Leu Lys Ser Tyr Leu Arg 100 105 110 Ser Leu Arg Pro Glu Ala Glu Asn Asn Pro Gly Arg Pro Pro Pro Thr 115 120 125 Leu Gln Glu Met Ile Gln Met Ala Ala Glu Ile Ala Asp Gly Met Ala 130 135 140 Tyr Leu Asn Ala Lys Lys Phe Val His Arg Asp Leu Ala Ala Arg Asn 145 150 155 160 Cys Met Val Ala His Asp Phe Thr Val Lys Ile Gly Asp Phe Gly Met 165 170 175 Thr Arg Asp Ile Tyr Glu Thr Asp Tyr Tyr Arg Lys Gly Gly Lys Gly 180 185 190 Leu Leu Pro Val Arg Trp Met Ala Pro Glu Ser Leu Lys Asp Gly Val 195 200 205 Phe Thr Thr Ser Ser Asp Met Trp Ser Phe Gly Val Val Leu Trp Glu 210 215 220 Ile Thr Ser Leu Ala Glu Gln Pro Tyr Gln Gly Leu Ser Asn Glu Gln 225 230 235 240 Val Leu Lys Phe Val Met Asp Gly Gly Tyr Leu Asp Gln Pro Asp Asn 245 250 255 Cys Pro Glu Arg Val Thr Asp Leu Met Arg Met Cys Trp Gln Phe Asn 260 265 270 Pro Lys Met Arg Pro Thr Phe Leu Glu Ile Val Asn Leu Leu Lys Asp 275 280 285 Asp Leu His Pro Ser Phe Pro Glu Val Ser Phe Phe His Ser Glu Glu 290 295 300 Asn Lys 305 13 299 PRT Homo sapiens 13 Leu Pro Glu Asp Pro Arg Trp Glu Leu Pro Arg Asp Arg Leu Val Leu 1 5 10 15 Gly Lys Pro Leu Gly Glu Gly Cys Phe Gly Gln Val Val Leu Ala Glu 20 25 30 Ala Ile Gly Leu Asp Lys Asp Lys Pro Asn Arg Val Thr Lys Val Ala 35 40 45 Val Lys Met Leu Lys Ser Asp Ala Thr Glu Lys Asp Leu Ser Asp Leu 50 55 60 Ile Ser Glu Met Glu Met Met Lys Met Ile Gly Lys His Lys Asn Ile 65 70 75 80 Ile Asn Leu Leu Gly Ala Cys Thr Gln Asp Gly Pro Leu Tyr Val Ile 85 90 95 Val Glu Tyr Ala Ser Lys Gly Asn Leu Arg Glu Tyr Leu Gln Ala Arg 100 105 110 Arg Pro Pro Gly Leu Glu Tyr Cys Tyr Asn Pro Ser His Asn Pro Glu 115 120 125 Glu Gln Leu Ser Ser Lys Asp Leu Val Ser Cys Ala Tyr Gln Val Ala 130 135 140 Arg Gly Met Glu Tyr Leu Ala Ser Lys Lys Cys Ile His Arg Asp Leu 145 150 155 160 Ala Ala Arg Asn Val Leu Val Thr Glu Asp Asn Val Met Lys Ile Ala 165 170 175 Asp Phe Gly Leu Ala Arg Asp Ile His His Ile Asp Tyr Tyr Lys Lys 180 185 190 Thr Thr Asn Gly Arg Leu Pro Val Lys Trp Met Ala Pro Glu Ala Leu 195 200 205 Phe Asp Arg Ile Tyr Thr His Gln Ser Asp Val Trp Ser Phe Gly Val 210 215 220 Leu Leu Trp Glu Ile Phe Thr Leu Gly Gly Ser Pro Tyr Pro Gly Val 225 230 235 240 Pro Val Glu Glu Leu Phe Lys Leu Leu Lys Glu Gly His Arg Met Asp 245 250 255 Lys Pro Ser Asn Cys Thr Asn Glu Leu Tyr Met Met Met Arg Asp Cys 260 265 270 Trp His Ala Val Pro Ser Gln Arg Pro Thr Phe Lys Gln Leu Val Glu 275 280 285 Asp Leu Asp Arg Ile Val Ala Leu Thr Ser Asn 290 295 14 279 PRT Homo sapiens 14 Pro Asn Gln Ala Leu Leu Arg Ile Leu Lys Glu Thr Glu Phe Lys Lys 1 5 10 15 Ile Lys Val Leu Gly Ser Gly Ala Phe Gly Thr Val Tyr Lys Gly Leu 20 25 30 Trp Ile Pro Glu Gly Glu Lys Val Lys Ile Pro Val Ala Ile Lys Glu 35 40 45 Leu Arg Glu Ala Thr Ser Pro Lys Ala Asn Lys Glu Ile Leu Asp Glu 50 55 60 Ala Tyr Val Met Ala Ser Val Asp Asn Pro His Val Cys Arg Leu Leu 65 70 75 80 Gly Ile Cys Leu Thr Ser Thr Val Gln Leu Ile Thr Gln Leu Met Pro 85 90 95 Phe Gly Cys Leu Leu Asp Tyr Val Arg Glu His Lys Asp Asn Ile Gly 100 105 110 Ser Gln Tyr Leu Leu Asn Trp Cys Val Gln Ile Ala Lys Gly Met Asn 115 120 125 Tyr Leu Glu Asp Arg Arg Leu Val His Arg Asp Leu Ala Ala Arg Asn 130 135 140 Val Leu Val Lys Thr Pro Gln His Val Lys Ile Thr Asp Phe Gly Leu 145 150 155 160 Ala Lys Leu Leu Gly Ala Glu Glu Lys Glu Tyr His Ala Glu Gly Gly 165 170 175 Lys Val Pro Ile Lys Trp Met Ala Leu Glu Ser Ile Leu His Arg Ile 180 185 190 Tyr Thr His Gln Ser Asp Val Trp Ser Tyr Gly Val Thr Val Trp Glu 195 200 205 Leu Met Thr Phe Gly Ser Lys Pro Tyr Asp Gly Ile Pro Ala Ser Glu 210 215 220 Ile Ser Ser Ile Leu Glu Lys Gly Glu Arg Leu Pro Gln Pro Pro Ile 225 230 235 240 Cys Thr Ile Asp Val Tyr Met Ile Met Val Lys Cys Trp Met Ile Asp 245 250 255 Ala Asp Ser Arg Pro Lys Phe Arg Glu Leu Ile Ile Glu Phe Ser Lys 260 265 270 Met Ala Arg Asp Pro Gln Arg 275 15 290 PRT Homo sapiens 15 Val Tyr Val Pro Asp Glu Trp Glu Val Ser Arg Glu Lys Ile Thr Leu 1 5 10 15 Leu Arg Glu Leu Gly Gln Gly Ser Phe Gly Met Val Tyr Glu Gly Asn 20 25 30 Ala Arg Asp Ile Ile Lys Gly Glu Ala Glu Thr Arg Val Ala Val Lys 35 40 45 Thr Val Asn Glu Ser Ala Ser Leu Arg Glu Arg Ile Glu Phe Leu Asn 50 55 60 Glu Ala Ser Val Met Lys Gly Phe Thr Cys His His Val Val Arg Leu 65 70 75 80 Leu Gly Val Val Ser Lys Gly Gln Pro Thr Leu Val Val Met Glu Leu 85 90 95 Met Ala His Gly Asp Leu Lys Ser Tyr Leu Arg Ser Leu Arg Pro Glu 100 105 110 Ala Glu Asn Asn Pro Gly Arg Pro Pro Pro Thr Leu Gln Glu Met Ile 115 120 125 Gln Met Ala Ala Glu Ile Ala Asp Gly Met Ala Tyr Leu Asn Ala Lys 130 135 140 Lys Phe Val His Arg Asp Leu Ala Ala Arg Asn Cys Met Val Ala His 145 150 155 160 Asp Phe Thr Val Lys Ile Gly Asp Phe Gly Met Thr Arg Asp Ile Tyr 165 170 175 Glu Thr Asp Tyr Tyr Arg Lys Gly Gly Lys Gly Leu Leu Pro Val Arg 180 185 190 Trp Met Ala Pro Glu Gly Leu Lys Asp Gly Val Phe Thr Thr Ser Ser 195 200 205 Asp Met Trp Ser Phe Gly Val Val Leu Trp Glu Ile Thr Ser Leu Ala 210 215 220 Glu Gln Pro Tyr Gln Gly Leu Ser Asn Glu Gln Val Leu Lys Phe Val 225 230 235 240 Met Asp Gly Gly Tyr Leu Asp Gln Pro Asp Asn Cys Pro Glu Arg Val 245 250 255 Thr Asp Leu Met Arg Met Cys Trp Gln Phe Asn Pro Lys Met Arg Pro 260 265 270 Thr Phe Leu Glu Ile Val Asn Leu Leu Lys Asp Asp Leu His Pro Ser 275 280 285 Phe Pro 290 16 293 PRT Homo sapiens 16 Leu Pro Tyr Asp Ser Arg Trp Glu Phe Pro Arg Asp Gly Leu Val Leu 1 5 10 15 Gly Arg Val Leu Gly Ser Gly Ala Phe Gly Lys Val Val Glu Gly Thr 20 25 30 Ala Tyr Gly Leu Ser Arg Ser Gln Pro Val Met Lys Val Ala Val Lys 35 40 45 Met Leu Lys Pro Thr Ala Arg Ser Ser Glu Lys Gln Ala Leu Met Ser 50 55 60 Glu Leu Lys Ile Met Thr His Leu Gly Pro His Leu Asn Ile Val Asn 65 70 75 80 Leu Leu Gly Ala Cys Thr Lys Ser Gly Pro Ile Tyr Ile Ile Thr Glu 85 90 95 Tyr Cys Phe Tyr Gly Asp Leu Val Asn Tyr Leu His Lys Asn Arg Asp 100 105 110 Ser Phe Leu Ser His His Pro Glu Ser Glu Gly Leu Thr Leu Leu Asp 115 120 125 Leu Leu Ser Phe Thr Tyr Gln Val Ala Arg Gly Met Glu Phe Leu Ala 130 135 140 Ser Lys Asn Cys Val His Arg Asp Leu Ala Ala Arg Asn Val Leu Leu 145 150 155 160 Ala Gln Gly Lys Ile Val Lys Ile Cys Asp Phe Gly Leu Ala Arg Asp 165 170 175 Ile Met His Asp Ser Asn Tyr Val Ser Lys Gly Ser Thr Phe Leu Pro 180 185 190 Val Lys Trp Met Ala Pro Glu Ser Ile Phe Asp Asn Leu Tyr Thr Thr 195 200 205 Leu Ser Asp Val Trp Ser Tyr Gly Ile Leu Leu Trp Glu Ile Phe Ser 210 215 220 Leu Gly Gly Thr Pro Tyr Pro Gly Met Met Val Asp Ser Thr Phe Tyr 225 230 235 240 Asn Lys Ile Lys Ser Gly Tyr Arg Met Ala Lys Pro Asp His Ala Thr 245 250 255 Ser Glu Val Tyr Glu Ile Met Val Lys Cys Trp Asn Ser Glu Pro Glu 260 265 270 Lys Arg Pro Ser Phe Tyr His Leu Ser Glu Ile Val Glu Asn Leu Leu 275 280 285 Pro Gly Gln Tyr Lys 290 17 294 PRT Homo sapiens 17 Pro Tyr Asp Ala Ser Lys Trp Glu Phe Pro Arg Asp Arg Leu Asn Leu 1 5 10 15 Gly Lys Pro Leu Gly Arg Gly Ala Phe Gly Gln Glu Ile Glu Ala Asp 20 25 30 Ala Phe Gly Ile Asp Lys Thr Ala Thr Cys Arg Thr Val Ala Val Lys 35 40 45 Met Leu Lys Glu Gly Ala Thr His Ser Glu His Arg Ala Leu Met Ser 50 55 60 Glu Leu Lys Ile Leu Ile His Ile Gly His His Leu Asn Val Val Asn 65 70 75 80 Leu Leu Gly Ala Cys Thr Lys Pro Gly Gly Pro Leu Met Val Ile Val 85 90 95 Glu Phe Cys Lys Phe Gly Asn Leu Ser Thr Tyr Leu Arg Ser Lys Arg 100 105 110 Asn Glu Phe Val Pro Tyr Lys Thr Lys Lys Asp Phe Leu Thr Leu Glu 115 120 125 His Leu Ile Cys Tyr Ser Phe Gln Val Ala Lys Gly Met Glu Phe Leu 130 135 140 Ala Ser Arg Lys Cys Ile His Arg Asp Leu Ala Ala Arg Asn Ile Leu 145 150 155 160 Leu Ser Glu Lys Asn Val Val Lys Ile Cys Asp Phe Gly Leu Ala Arg 165 170 175 Asp Ile Tyr Lys Asp Pro Asp Tyr Val Arg Lys Gly Asp Ala Arg Leu 180 185 190 Pro Leu Lys Trp Met Ala Pro Glu Thr Ile Phe Asp Arg Val Tyr Thr 195 200 205 Ile Gln Ser Asp Val Trp Ser Phe Gly Val Leu Leu Trp Glu Ile Phe 210 215 220 Ser Leu Gly Ala Ser Pro Tyr Pro Gly Val Lys Ile Asp Glu Glu Phe 225 230 235 240 Cys Arg Arg Leu Lys Glu Gly Thr Arg Met Arg Ala Pro Asp Tyr Thr 245 250 255 Thr Pro Glu Met Tyr Gln Thr Met Leu Asp Cys Trp His Gly Glu Pro 260 265 270 Ser Gln Arg Pro Thr Phe Ser Glu Leu Val Glu His Leu Gly Asn Leu 275 280 285 Leu Gln Ala Asn Ala Gln 290 18 288 PRT Homo sapiens 18 His Ser Thr Ser Asp Lys Met His Phe Pro Arg Ser Ser Leu Gln Pro 1 5 10 15 Ile Thr Thr Leu Gly Lys Ser Glu Phe Gly Glu Val Phe Leu Ala Lys 20 25 30 Ala Gln Gly Leu Glu Glu Gly Val Ala Glu Thr Leu Val Leu Val Lys 35 40 45 Ser Leu Gln Ser Lys Asp Glu Gln Gln Gln Leu Asp Phe Arg Arg Glu 50 55 60 Leu Glu Met Phe Gly Lys Leu Asn His Ala Asn Val Val Arg Leu Leu 65 70 75 80 Gly Leu Cys Arg Glu Ala Glu Pro His Tyr Met Val Leu Glu Tyr Val 85 90 95 Asp Leu Gly Asp Leu Lys Gln Phe Leu Arg Ile Ser Lys Ser Lys Asp 100 105 110 Glu Lys Leu Lys Ser Gln Pro Leu Ser Thr Lys Gln Lys Val Ala Leu 115 120 125 Cys Thr Gln Val Ala Leu Gly Met Glu His Leu Ser Asn Asn Arg Phe 130 135 140 Val His Lys Asp Leu Ala Ala Arg Asn Cys Leu Val Ser Ala Gln Arg 145 150 155 160 Gln Val Lys Val Ser Ala Leu Gly Leu Ser Lys Asp Val Tyr Asn Ser 165 170 175 Glu Tyr Tyr His Phe Arg Gln Ala Trp Val Pro Leu Arg Trp Met Ser 180 185 190 Pro Glu Ala Ile Leu Glu Gly Asp Phe Ser Thr Lys Ser Asp Val Trp 195 200 205 Ala Phe Gly Val Leu Met Trp Glu Val Phe Thr His Gly Glu Met Pro 210 215 220 His Gly Gly Gln Ala Asp Asp Glu Val Leu Ala Asp Leu Gln Ala Gly 225 230 235 240 Lys Ala Arg Leu Pro Gln Pro Glu Gly Cys Pro Ser Lys Leu Tyr Arg 245 250 255 Leu Met Gln Arg Cys Trp Ala Leu Ser Pro Lys Asp Arg Pro Ser Phe 260 265 270 Ser Glu Ile Ala Ser Ala Leu Gly Asp Ser Thr Val Asp Ser Lys Pro 275 280 285 19 282 PRT Homo sapiens 19 Ala Val Gln His Val Val Ile Gly Pro Ser Ser Leu Ile Val His Phe 1 5 10 15 Asn Glu Val Ile Gly Arg Gly His Phe Gly Cys Val Tyr His Gly Thr 20 25 30 Leu Leu Asp Asn Asp Gly Lys Lys Ile His Cys Ala Val Lys Ser Leu 35 40 45 Asn Arg Ile Thr Asp Ile Gly Glu Val Ser Gln Phe Leu Thr Glu Gly 50 55 60 Ile Ile Met Lys Asp Phe Ser His Pro Asn Val Leu Ser Leu Leu Gly 65 70 75 80 Ile Cys Leu Arg Ser Glu Gly Ser Pro Leu Val Val Leu Pro Tyr Met 85 90 95 Lys His Gly Asp Leu Arg Asn Phe Ile Arg Asn Glu Thr His Asn Pro 100 105 110 Thr Val Lys Asp Leu Ile Gly Phe Gly Leu Gln Val Ala Lys Gly Met 115 120 125 Lys Tyr Leu Ala Ser Lys Lys Phe Val His Arg Asp Leu Ala Ala Arg 130 135 140 Asn Cys Met Leu Asp Glu Lys Phe Thr Val Lys Val Ala Asp Phe Gly 145 150 155 160 Leu Ala Arg Asp Met Tyr Asp Lys Glu Tyr Tyr Ser Val His Asn Lys 165 170 175 Thr Gly Ala Lys Leu Pro Val Lys Trp Met Ala Leu Glu Ser Leu Gln 180 185 190 Thr Gln Lys Phe Thr Thr Lys Ser Asp Val Trp Ser Phe Gly Val Val 195 200 205 Leu Trp Glu Leu Met Thr Arg Gly Ala Pro Pro Tyr Pro Asp Val Asn 210 215 220 Thr Phe Asp Ile Thr Val Tyr Leu Leu Gln Gly Arg Arg Leu Leu Gln 225 230 235 240 Pro Glu Tyr Cys Pro Asp Pro Leu Tyr Glu Val Met Leu Lys Cys Trp 245 250 255 His Pro Lys Ala Glu Met Arg Pro Ser Phe Ser Glu Leu Val Ser Arg 260 265 270 Ile Ser Ala Ile Phe Ser Thr Phe Ile Gly 275 280 20 294 PRT Homo sapiens 20 Phe Ser Asp Ala Cys Val His His Ile Lys Arg Arg Asp Ile Val Leu 1 5 10 15 Lys Trp Glu Leu Gly Glu Gly Ala Phe Gly Lys Val Phe Leu Ala Glu 20 25 30 Cys His Asn Leu Leu Pro Glu Gln Asp Lys Met Leu Val Ala Val Lys 35 40 45 Ala Leu Lys Glu Ala Ser Glu Ser Ala Arg Gln Asp Phe Gln Arg Glu 50 55 60 Ala Glu Leu Leu Thr Met Leu Gln His Gln His Ile Val Arg Phe Phe 65 70 75 80 Gly Val Cys Thr Glu Gly Arg Pro Leu Leu Met Val Phe Glu Tyr Met 85 90 95 Arg His Gly Asp Leu Asn Arg Phe Leu Arg Ser His Gly Pro Asp Ala 100 105 110 Lys Leu Leu Ala Gly Gly Glu Asp Val Ala Pro Gly Pro Leu Gly Leu 115 120 125 Gly Gln Leu Leu Ala Val Ala Ser Gln Val Ala Ala Gly Met Val Tyr 130 135 140 Leu Ala Gly Leu His Phe Val His Arg Asp Leu Ala Thr Arg Asn Cys 145 150 155 160 Leu Val Gly Gln Gly Leu Val Val Lys Ile Gly Asp Phe Gly Met Ser 165 170 175 Arg Asp Ile Tyr Ser Thr Asp Tyr Tyr Arg Val Gly Gly Arg Thr Met 180 185 190 Leu Pro Ile Arg Trp Met Pro Pro Glu Ser Ile Leu Tyr Arg Lys Phe 195 200 205 Thr Thr Glu Ser Asp Val Trp Ser Phe Gly Val Val Leu Trp Glu Ile 210 215 220 Phe Thr Tyr Gly Lys Gln Pro Trp Tyr Gln Leu Ser Asn Thr Glu Ala 225 230 235 240 Ile Asp Cys Ile Thr Gln Gly Arg Glu Leu Glu Arg Pro Arg Ala Cys 245 250 255 Pro Pro Glu Val Tyr Ala Ile Met Arg Gly Cys Trp Gln Arg Glu Pro 260 265 270 Gln Gln Arg His Ser Ile Lys Asp Val His Ala Arg Leu Gln Ala Leu 275 280 285 Ala Gln Ala Pro Pro Val 290 21 290 PRT Homo sapiens 21 Lys Glu Lys Leu Arg Asp Val Met Val Asp Arg His Lys Val Ala Leu 1 5 10 15 Gly Lys Thr Leu Gly Glu Gly Glu Phe Gly Ala Val Met Glu Gly Gln 20 25 30 Leu Asn Gln Asp Asp Ser Ile Leu Lys Val Ala Val Lys Thr Met Lys 35 40 45 Ile Ala Ile Cys Thr Arg Ser Glu Leu Glu Asp Phe Leu Ser Glu Ala 50 55 60 Val Cys Met Lys Glu Phe Asp His Pro Asn Val Met Arg Leu Ile Gly 65 70 75 80 Val Cys Phe Gln Gly Ser Glu Arg Glu Ser Phe Pro Ala Pro Val Val 85 90 95 Ile Leu Pro Phe Met Lys His Gly Asp Leu His Ser Phe Leu Leu Tyr 100 105 110 Ser Arg Leu Gly Asp Gln Pro Val Tyr Leu Pro Thr Gln Met Leu Val 115 120 125 Lys Phe Met Ala Asp Ile Ala Ser Gly Met Glu Tyr Leu Ser Thr Lys 130 135 140 Arg Phe Ile His Arg Asp Leu Ala Ala Arg Asn Cys Met Leu Asn Glu 145 150 155 160 Asn Met Ser Val Cys Val Ala Asp Phe Gly Leu Ser Lys Lys Ile Tyr 165 170 175 Asn Gly Asp Tyr Tyr Arg Gln Gly Arg Ile Ala Lys Met Pro Val Lys 180 185 190 Trp Ile Ala Ile Glu Ser Leu Ala Asp Arg Val Tyr Thr Ser Lys Ser 195 200 205 Asp Val Trp Ser Phe Gly Val Thr Met Trp Glu Ile Ala Thr Arg Gly 210 215 220 Gln Thr Pro Tyr Pro Gly Val Glu Asn Ser Glu Ile Tyr Asp Tyr Leu 225 230 235 240 Arg Gln Gly Asn Arg Leu Lys Gln Pro Ala Asp Cys Leu Asp Gly Leu 245 250 255 Tyr Ala Leu Met Ser Arg Cys Trp Glu Leu Asn Pro Gln Asp Arg Pro 260 265 270 Ser Phe Thr Glu Leu Arg Glu Asp Leu Glu Asn Thr Leu Lys Ala Leu 275 280 285 Pro Pro 290 22 291 PRT Homo sapiens 22 Pro Glu Pro Leu Ser Tyr Pro Val Leu Glu Trp Glu Asp Ile Thr Phe 1 5 10 15 Glu Asp Leu Ile Gly Glu Gly Asn Phe Gly Gln Val Ile Arg Ala Met 20 25 30 Ile Lys Lys Asp Gly Leu Lys Met Asn Ala Ala Ile Lys Met Leu Lys 35 40 45 Glu Tyr Ala Ser Glu Asn Asp His Arg Asp Phe Ala Gly Glu Leu Glu 50 55 60 Val Leu Cys Lys Leu Gly His His Pro Asn Ile Ile Asn Leu Leu Gly 65 70 75 80 Ala Cys Lys Asn Arg Gly Tyr Leu Tyr Ile Ala Ile Glu Tyr Ala Pro 85 90 95 Tyr Gly Asn Leu Leu Asp Phe Leu Arg Lys Ser Arg Val Leu Glu Thr 100 105 110 Asp Pro Ala Phe Ala Arg Glu His Gly Thr Ala Ser Thr Leu Ser Ser 115 120 125 Arg Gln Leu Leu Arg Phe Ala Ser Asp Ala Ala Asn Gly Met Gln Tyr 130 135 140 Leu Ser Glu Lys Gln Phe Ile His Arg Asp Leu Ala Ala Arg Asn Val 145 150 155 160 Leu Val Gly Glu Asn Leu Ala Ser Lys Ile Ala Asp Phe Gly Leu Ser 165 170 175 Arg Gly Glu Glu Val Tyr Val Lys Lys Thr Met Gly Arg Leu Pro Val 180 185 190 Arg Trp Met Ala Ile Glu Ser Leu Asn Tyr Ser Val Tyr Thr Thr Lys 195 200 205 Ser Asp Val Trp Ser Phe Gly Val Leu Leu Trp Glu Ile Val Ser Leu 210 215 220 Gly Gly Thr Pro Tyr Cys Gly Met Thr Cys Ala Glu Leu Tyr Glu Lys 225 230 235 240 Leu Pro Gln Gly Tyr Arg Met Glu Gln Pro Arg Asn Cys Asp Asp Glu 245 250 255 Val Tyr Glu Leu Met Arg Gln Cys Trp Arg Asp Arg Pro Tyr Glu Arg 260 265 270 Pro Pro Phe Ala Gln Ile Ala Leu Gln Leu Gly Arg Met Leu Glu Ala 275 280 285 Arg Lys Ala 290 23 279 PRT Homo sapiens 23 Trp Ser Asn Phe Pro Ser Arg Glu Leu Asp Pro Ala Trp Leu Met Val 1 5 10 15 Asp Thr Val Ile Gly Glu Gly Glu Phe Gly Glu Val Tyr Arg Gly Thr 20 25 30 Leu Arg Leu Pro Ser Gln Asp Cys Lys Thr Val Ala Ile Lys Thr Leu 35 40 45 Lys Asp Thr Ser Pro Gly Gly Gln Trp Trp Asn Phe Leu Arg Glu Ala 50 55 60 Thr Ile Met Gly Gln Phe Ser His Pro His Ile Leu His Leu Glu Gly 65 70 75 80 Val Val Thr Lys Arg Lys Pro Ile Met Ile Ile Thr Glu Phe Met Glu 85 90 95 Asn Gly Ala Leu Asp Ala Phe Leu Arg Glu Arg Glu Asp Gln Leu Val 100 105 110 Pro Gly Gln Leu Val Ala Met Leu Gln Gly Ile Ala Ser Gly Met Asn 115 120 125 Tyr Leu Ser Asn His Asn Tyr Val His Arg Asp Leu Ala Ala Arg Asn 130 135 140 Ile Leu Val Asn Gln Asn Leu Cys Cys Lys Val Ser Asp Phe Gly Leu 145 150 155 160 Thr Arg Leu Leu Asp Asp Phe Asp Gly Thr Tyr Glu Thr Gln Gly Gly 165 170 175 Lys Ile Pro Ile Arg Trp Thr Ala Pro Glu Ala Ile Ala His Arg Ile 180 185 190 Phe Thr Thr Ala Ser Asp Val Trp Ser Phe Gly Ile Val Met Trp Glu 195 200 205 Val Leu Ser Phe Gly Asp Lys Pro Tyr Gly Glu Met Ser Asn Gln Glu 210 215 220 Val Met Lys Ser Ile Glu Asp Gly Tyr Arg Leu Pro Pro Pro Val Asp 225 230 235 240 Cys Pro Ala Pro Leu Tyr Glu Leu Met Lys Asn Cys Trp Ala Tyr Asp 245 250 255 Arg Ala Arg Arg Pro His Phe Gln Lys Leu Gln Ala His Leu Glu Gln 260 265 270 Leu Leu Ala Asn Pro His Ser 275 24 291 PRT Homo sapiens 24 Lys Gly Lys Val Lys Asp Ile Ala Ile Ser Arg Glu Arg Ile Thr Leu 1 5 10 15 Lys Asp Val Leu Gln Glu Gly Thr Phe Gly Arg Ile Phe His Gly Ile 20 25 30 Leu Ile Asp Glu Lys Asp Pro Asn Lys Glu Lys Gln Ala Phe Val Lys 35 40 45 Thr Val Lys Asp Gln Ala Ser Glu Ile Gln Val Thr Met Met Leu Thr 50 55 60 Glu Ser Cys Lys Leu Arg Gly Leu His His Arg Asn Leu Leu Pro Ile 65 70 75 80 Thr His Val Cys Ile Glu Glu Gly Glu Lys Pro Met Val Ile Leu Pro 85 90 95 Tyr Met Asn Trp Gly Asn Leu Lys Leu Phe Leu Arg Gln Cys Lys Leu 100 105 110 Val Glu Ala Asn Asn Pro Gln Ala Ile Ser Gln Gln Asp Leu Val His 115 120 125 Met Ala Ile Gln Ile Ala Cys Gly Met Ser Tyr Leu Ala Arg Arg Glu 130 135 140 Val Ile His Lys Asp Leu Ala Ala Arg Asn Cys Val Ile Asp Asp Thr 145 150 155 160 Leu Gln Val Lys Ile Thr Asp Asn Ala Leu Ser Arg Asp Leu Phe Pro 165 170 175 Met Asp Tyr His Cys Leu Gly Asp Asn Glu Asn Arg Pro Val Arg Trp 180 185 190 Met Ala Leu Glu Ser Leu Val Asn Asn Glu Phe Ser Ser Ala Ser Asp 195 200 205 Val Trp Ala Phe Gly Val Asn Ser Leu Trp Glu Leu Met Thr Leu Gly 210 215 220 Gln Thr Pro Tyr Thr Leu Asp Ile Asp Pro Phe Glu Met Ala Ala Tyr 225 230 235 240 Leu Lys Asp Gly Tyr Arg Ile Ala Gln Pro Ile Thr Cys Pro Asp Glu 245 250 255 Leu Phe Ala Val Met Ala Cys Cys Trp Ala Leu Asp Pro Glu Glu Arg 260 265 270 Pro Arg Phe Gln Gln Leu Val Gln Cys Leu Thr Glu Phe His Ala Ala 275 280 285 Leu Gly Ala 290 25 317 PRT Homo sapiens 25 Gly Asp Gly Pro Pro Arg Val Asp Phe Pro Arg Ser Arg Leu Arg Phe 1 5 10 15 Lys Glu Lys Leu Gly Phe Gly Gln Phe Gly Glu Val His Leu Cys Glu 20 25 30 Val Asp Ser Pro Gln Asp Leu Val Ser Leu Asp Phe Pro Leu Asn Val 35 40 45 Arg Lys Gly His Pro Leu Leu Val Ala Val Lys Ile Leu Arg Pro Asp 50 55 60 Ala Thr Lys Asn Ala Arg Asn Asp Phe Leu Lys Glu Val Lys Ile Met 65 70 75 80 Ser Arg Leu Lys Asp Pro Asn Ile Ile Arg Leu Leu Gly Val Cys Val 85 90 95 Gln Asp Asp Pro Leu Cys Met Ile Thr Asp Tyr Met Glu Asn Gly Asp 100 105 110 Leu Asn Gln Phe Leu Ser Ala His Gln Leu Glu Asp Lys Ala Ala Glu 115 120 125 Gly Ala Pro Gly Asp Gly Gln Ala Ala Gln Gly Pro Thr Ile Ser Tyr 130 135 140 Pro Met Leu Leu His Val Ala Ala Gln Ile Ala Ser Gly Met Arg Tyr 145 150 155 160 Leu Ala Thr Leu Asn Phe Val His Arg Asp Leu Ala Thr Arg Asn Cys 165 170 175 Leu Val Gly Glu Asn Phe Thr Ile Lys Ile Ala Asp Phe Gly Met Ser 180 185 190 Arg Asn Leu Tyr Ala Gly Asp Tyr Tyr Arg Val Gln Gly Arg Ala Val 195 200 205 Leu Pro Ile Arg Trp Met Ala Trp Glu Cys Ile Leu Met Gly Lys Phe 210 215 220 Thr Thr Ala Ser Asp Val Trp Ala Phe Gly Val Thr Val Trp Glu Val 225 230 235 240 Leu Met Leu Cys Arg Ala Gln Pro Phe Gly Gln Leu Thr Asp Glu Gln 245 250 255 Val Ile Glu Asn Ala Gly Glu Phe Phe Arg Asp Gln Gly Arg Gln Val 260 265 270 Tyr Leu Ser Arg Pro Pro Ala Cys Pro Gln Gly Leu Tyr Glu Leu Met 275 280 285 Leu Arg Cys Trp Gly Arg Glu Ser Glu Gln Arg Pro Pro Phe Ser Gln 290 295 300 Leu His Arg Phe Leu Ala Glu Asp Ala Leu Asn Thr Val 305 310 315 26 293 PRT Homo sapiens 26 Glu Glu Ile Glu Asn Leu Pro Ala Phe Pro Arg Glu Lys Leu Thr Leu 1 5 10 15 Arg Leu Leu Leu Gly Ser Gly Ala Phe Gly Glu Val Tyr Glu Gly Thr 20 25 30 Ala Val Asp Ile Leu Gly Val Gly Ser Gly Glu Ile Lys Val Ala Val 35 40 45 Lys Thr Leu Lys Lys Gly Ser Thr Asp Gln Glu Lys Ile Glu Phe Leu 50 55 60 Lys Glu Ala His Leu Met Ser Lys Phe Asn His Pro Asn Ile Leu Lys 65 70 75 80 Gln Leu Gly Val Cys Leu Leu Asn Glu Pro Gln Tyr Ile Ile Leu Glu 85 90 95 Leu Met Glu Gly Gly Asp Leu Leu Thr Tyr Leu Arg Lys Ala Arg Met 100 105 110 Ala Thr Phe Tyr Gly Pro Leu Leu Thr Leu Val Asp Leu Val Asp Leu 115 120 125 Cys Val Asp Ile Ser Lys Gly Cys Val Tyr Leu Glu Arg Met His Phe 130 135 140 Ile His Arg Asp Leu Ala Ala Arg Asn Cys Leu Val Ser Val Lys Asp 145 150 155 160 Tyr Thr Ser Pro Arg Ile Val Lys Ile Gly Asp Phe Gly Leu Ala Arg 165 170 175 Asp Ile Tyr Lys Asn Asp Tyr Tyr Arg Lys Arg Gly Glu Gly Leu Leu 180 185 190 Pro Val Arg Trp Met Ala Pro Glu Ser Leu Met Asp Gly Ile Phe Thr 195 200 205 Thr Gln Ser Asp Val Trp Ser Phe Gly Ile Leu Ile Trp Glu Ile Leu 210 215 220 Thr Leu Gly His Gln Pro Tyr Pro Ala His Ser Asn Leu Asp Val Leu 225 230 235 240 Asn Tyr Val Gln Thr Gly Gly Arg Leu Glu Pro Pro Arg Asn Cys Pro 245 250 255 Asp Asp Leu Trp Asn Leu Met Thr Gln Cys Trp Ala Gln Glu Pro Asp 260 265 270 Gln Arg Pro Thr Phe His Arg Ile Gln Asn Gln Leu Gln Leu Phe Arg 275 280 285 Asn Phe Phe Leu Asn 290 27 304 PRT Homo sapiens 27 Ile Leu Glu Asp Pro Lys Trp Glu Phe Pro Arg Lys Asn Leu Val Leu 1 5 10 15 Gly Lys Thr Leu Gly Glu Gly Glu Phe Gly Lys Val Val Lys Ala Thr 20 25 30 Ala Phe His Leu Lys Gly Arg Ala Gly Tyr Thr Thr Val Ala Val Lys 35 40 45 Met Leu Lys Glu Asn Ala Ser Pro Ser Glu Leu Arg Asp Leu Leu Ser 50 55 60 Glu Phe Asn Val Leu Lys Gln Val Asn His Pro His Val Ile Lys Leu 65 70 75 80 Tyr Gly Ala Cys Ser Gln Asp Gly Pro Leu Leu Leu Ile Val Glu Tyr 85 90 95 Ala Lys Tyr Gly Ser Leu Arg Gly Phe Leu Arg Glu Ser Arg Lys Val 100 105 110 Gly Pro Gly Tyr Leu Gly Ser Gly Gly Ser Arg Asn Ser Ser Ser Leu 115 120 125 Asp His Pro Asp Glu Arg Ala Leu Thr Met Gly Asp Leu Ile Ser Phe 130 135 140 Ala Trp Gln Ile Ser Gln Gly Met Gln Tyr Leu Ala Glu Met Lys Leu 145 150 155 160 Val His Arg Asp Leu Ala Ala Arg Asn Ile Leu Val Ala Glu Gly Arg 165 170 175 Lys Met Lys Ile Ser Asp Phe Gly Leu Ser Arg Asp Val Tyr Glu Glu 180 185 190 Asp Ser Tyr Val Lys Arg Ser Gln Gly Arg Ile Pro Val Lys Trp Met 195 200 205 Ala Ile Glu Ser Leu Phe Asp His Ile Tyr Thr Thr Gln Ser Asp Val 210 215 220 Trp Ser Phe Gly Val Leu Leu Trp Glu Ile Val Thr Leu Gly Gly Asn 225 230 235 240 Pro Tyr Pro Gly Ile Pro Pro Glu Arg Leu Phe Asn Leu Leu Lys Thr 245 250 255 Gly His Arg Met Glu Arg Pro Asp Asn Cys Ser Glu Glu Met Tyr Arg 260 265 270 Leu Met Leu Gln Cys Trp Lys Gln Glu Pro Asp Lys Arg Pro Val Phe 275 280 285 Ala Asp Ile Ser Lys Asp Leu Glu Lys Met Met Val Lys Arg Arg Asp 290 295 300 28 290 PRT Homo sapiens 28 Pro Leu Pro Pro Gly Val Thr Glu Val Ser Pro Ala Asn Val Thr Leu 1 5 10 15 Leu Arg Ala Leu Gly His Gly Ala Phe Gly Glu Val Tyr Glu Gly Leu 20 25 30 Val Ile Gly Leu Pro Gly Asp Ser Ser Pro Leu Gln Val Ala Ile Lys 35 40 45 Thr Leu Pro Glu Leu Cys Ser Pro Gln Asp Glu Leu Asp Phe Leu Met 50 55 60 Glu Ala Leu Ile Ile Ser Lys Phe Arg His Gln Asn Ile Val Arg Cys 65 70 75 80 Val Gly Leu Ser Leu Arg Ala Thr Pro Arg Leu Ile Leu Leu Glu Leu 85 90 95 Met Ser Gly Gly Asp Met Lys Ser Phe Leu Arg His Ser Arg Pro His 100 105 110 Leu Gly Gln Pro Ser Pro Leu Val Met Arg Asp Leu Leu Gln Leu Ala 115 120 125 Gln Asp Ile Ala Gln Gly Cys His Tyr Leu Glu Glu Asn His Phe Ile 130 135 140 His Arg Asp Ile Ala Ala Arg Asn Cys Leu Leu Ser Cys Ala Gly Pro 145 150 155 160 Ser Arg Val Ala Lys Ile Gly Asp Phe Gly Met Ala Arg Asp Ile Tyr 165 170 175 Arg Ala Ser Tyr Tyr Arg Arg Gly Asp Arg Ala Leu Leu Pro Val Lys 180 185 190 Trp Met Pro Pro Glu Ala Phe Leu Glu Gly Ile Phe Thr Ser Lys Thr 195 200 205 Asp Ser Trp Ser Phe Gly Val Leu Leu Trp Glu Ile Phe Ser Leu Gly 210 215 220 Tyr Met Pro Tyr Pro Gly Arg Thr Asn Gln Glu Val Leu Asp Phe Val 225 230 235 240 Val Gly Gly Gly Arg Met Asp Pro Pro Arg Gly Cys Pro Gly Pro Val 245 250 255 Tyr Arg Ile Met Thr Gln Cys Trp Gln His Glu Pro Glu Leu Arg Pro 260 265 270 Ser Phe Ala Ser Ile Leu Glu Arg Leu Gln Tyr Cys Thr Gln Asp Pro 275 280 285 Asp Val 290 29 296 PRT Homo sapiens 29 Lys Pro Lys Ser Lys Ala Lys Glu Leu Pro Leu Ser Ala Val Arg Phe 1 5 10 15 Met Glu Glu Leu Gly Glu Cys Ala Phe Gly Lys Ile Tyr Lys Gly His 20 25 30 Leu Tyr Leu Pro Gly Met Asp His Ala Gln Leu Val Ala Ile Lys Thr 35 40 45 Leu Lys Asp Tyr Asn Asn Pro Gln Gln Trp Met Glu Phe Gln Gln Glu 50 55 60 Ala Ser Leu Met Ala Glu Leu His His Pro Asn Ile Val Cys Leu Leu 65 70 75 80 Gly Ala Val Thr Gln Glu Gln Pro Val Cys Met Leu Phe Glu Tyr Ile 85 90 95 Asn Gln Gly Asp Leu His Glu Phe Leu Ile Met Arg Ser Pro His Ser 100 105 110 Asp Val Gly Cys Ser Ser Asp Glu Asp Gly Thr Val Lys Ser Ser Leu 115 120 125 Asp His Gly Asp Phe Leu His Ile Ala Ile Gln Ile Ala Ala Gly Met 130 135 140 Glu Tyr Leu Ser Ser His Phe Phe Val His Lys Asp Leu Ala Ala Arg 145 150 155 160 Asn Ile Leu Ile Gly Glu Gln Leu His Val Lys Ile Ser Asp Leu Gly 165 170 175 Leu Ser Arg Glu Ile Tyr Ser Ala Asp Tyr Tyr Arg Val Gln Ser Lys 180 185 190 Ser Leu Leu Pro Ile Arg Trp Met Pro Pro Glu Ala Ile Met Tyr Gly 195 200 205 Lys Phe Ser Ser Asp Ser Asp Ile Trp Ser Phe Gly Val Val Leu Trp 210 215 220 Glu Ile Phe Ser Phe Gly Leu Gln Pro Tyr Tyr Gly Phe Ser Asn Gln 225 230 235 240 Glu Val Ile Glu Met Val Arg Lys Arg Gln Leu Leu Pro Cys Ser Glu 245 250 255 Asp Cys Pro Pro Arg Met Tyr Ser Leu Met Thr Glu Cys Trp Asn Glu 260 265 270 Ile Pro Ser Arg Arg Pro Arg Phe Lys Asp Ile His Val Arg Leu Arg 275 280 285 Ser Trp Glu Gly Leu Ser Ser His 290 295 30 304 PRT Mus sp. 30 Asn Pro Lys Leu Leu Ser Leu Glu Tyr Pro Arg Asn Asn Ile Glu Tyr 1 5 10 15 Val Arg Asp Ile Gly Glu Gly Ala Phe Gly Arg Val Phe Gln Ala Arg 20 25 30 Ala Pro Gly Leu Leu Pro Tyr Glu Pro Phe Thr Met Val Ala Val Lys 35 40 45 Met Leu Lys Glu Glu Ala Ser Ala Asp Met Gln Ala Asp Phe Gln Arg 50 55 60 Glu Ala Ala Leu Met Ala Glu Phe Asp Asn Pro Asn Ile Val Lys Leu 65 70 75 80 Leu Gly Val Cys Ala Val Gly Lys Pro Met Cys Leu Leu Phe Glu Tyr 85 90 95 Met Ala Tyr Gly Asp Leu Asn Glu Phe Leu Arg Ser Met Ser Pro His 100 105 110 Thr Val Cys Ser Leu Ser His Ser Asp Leu Ser Thr Arg Ala Arg Val 115 120 125 Ser Ser Pro Gly Pro Pro Pro Leu Ser Cys Ala Glu Gln Leu Cys Ile 130 135 140 Ala Arg Gln Val Ala Ala Gly Met Ala Tyr Leu Ser Glu Arg Lys Phe 145 150 155 160 Val His Arg Asp Leu Ala Thr Arg Asn Cys Leu Val Gly Glu Thr Met 165 170 175 Val Val Lys Ile Ala Asp Phe Gly Leu Ser Arg Asn Ile Tyr Ser Ala 180 185 190 Asp Tyr Tyr Lys Ala Asp Gly Asn Asp Ala Ile Pro Ile Arg Trp Met 195 200 205 Pro Pro Glu Ser Ile Phe Tyr Asn Arg Tyr Thr Thr Glu Ser Asp Val 210 215 220 Trp Ala Tyr Gly Val Val Leu Trp Glu Ile Phe Ser Tyr Gly Leu Gln 225 230 235 240 Pro Tyr Tyr Gly Met Ala His Glu Glu Val Ile Tyr Tyr Val Arg Asp 245 250 255 Gly Asn Ile Leu Ala Cys Pro Glu Asn Cys Pro Leu Glu Leu Tyr Asn 260 265 270 Leu Met Arg Leu Cys Trp Ser Lys Leu Pro Ala Asp Arg Pro Ser Phe 275 280 285 Cys Ser Ile His Arg Ile Leu Gln Arg Met Cys Glu Arg Ala Glu Gly 290 295 300 31 300 PRT Homo sapiens 31 Leu Pro Glu Asp Pro Arg Trp Glu Leu Pro Arg Asp Arg Leu Val Leu 1 5 10 15 Gly Lys Pro Leu Gly Glu Gly Cys Phe Gly Gln Val Val Leu Ala Glu 20 25 30 Ala Ile Gly Leu Asp Lys Asp Lys Pro Asn Arg Val Thr Lys Val Ala 35 40 45 Val Lys Met Leu Lys Ser Asp Ala Thr Glu Lys Asp Leu Ser Asp Leu 50 55 60 Ile Ser Glu Met Glu Met Met Lys Met Ile Gly Lys His Lys Asn Ile 65 70 75 80 Ile Asn Leu Leu Gly Ala Cys Thr Gln Asp Gly Pro Leu Tyr Val Ile 85 90 95 Val Glu Tyr Ala Ser Lys Gly Asn Leu Arg Glu Tyr Leu Gln Ala Arg 100 105 110 Arg Pro Pro Gly Leu Glu Tyr Cys Tyr Asn Pro Ser His Asn Pro Glu 115 120 125 Glu Gln Leu Ser Ser Lys Asp Leu Val Ser Cys Ala Tyr Gln Val Ala 130 135 140 Arg Gly Met Glu Tyr Leu Ala Ser Lys Lys Cys Ile His Arg Asp Leu 145 150 155 160 Ala Ala Arg Asn Val Leu Val Thr Glu Asp Asn Val Met Lys Ile Ala 165 170 175 Asp Phe Gly Leu Ala Arg Asp Ile His His Ile Asp Tyr Tyr Lys Lys 180 185 190 Thr Thr Asn Gly Arg Leu Pro Val Lys Trp Met Ala Pro Glu Ala Leu 195 200 205 Phe Asp Arg Ile Tyr Thr His Gln Ser Asp Val Trp Ser Phe Gly Val 210 215 220 Leu Leu Trp Glu Ile Phe Thr Leu Gly Gly Ser Pro Tyr Pro Gly Val 225 230 235 240 Pro Val Glu Glu Leu Phe Lys Leu Leu Lys Glu Gly His Arg Met Asp 245 250 255 Lys Pro Ser Asn Cys Thr Asn Glu Leu Tyr Met Met Met Arg Asp Cys 260 265 270 Trp His Ala Val Pro Ser Gln Arg Pro Thr Phe Lys Gln Leu Val Glu 275 280 285 Asp Leu Asp Arg Ile Val Ala Leu Thr Ser Asn Gln 290 295 300 32 273 PRT Homo sapiens 32 Gly Leu Ala Lys Asp Ala Trp Glu Ile Pro Arg Glu Ser Leu Arg Leu 1 5 10 15 Glu Val Lys Leu Gly Gln Gly Cys Phe Gly Glu Val Trp Met Gly Thr 20 25 30 Trp Asn Gly Thr Thr Arg Val Ala Ile Lys Thr Leu Lys Pro Gly Thr 35 40 45 Met Ser Pro Glu Ala Phe Leu Gln Glu Ala Gln Val Met Lys Lys Leu 50 55 60 Arg His Glu Lys Leu Val Gln Leu Tyr Ala Val Val Ser Glu Glu Pro 65 70 75 80 Ile Tyr Ile Val Thr Glu Tyr Met Ser Lys Gly Ser Leu Leu Asp Phe 85 90 95 Leu Lys Gly Glu Thr Gly Lys Tyr Leu Arg Leu Pro Gln Leu Val Asp 100 105 110 Met Ala Ala Gln Ile Ala Ser Gly Met Ala Tyr Val Glu Arg Met Asn 115 120 125 Tyr Val His Arg Asp Leu Arg Ala Ala Asn Ile Leu Val Gly Glu Asn 130 135 140 Leu Val Cys Lys Val Ala Asp Phe Gly Leu Ala Arg Leu Ile Glu Asp 145 150 155 160 Asn Glu Tyr Thr Ala Arg Gln Gly Ala Lys Phe Pro Ile Lys Trp Thr 165 170 175 Ala Pro Glu Ala Ala Leu Tyr Gly Arg Phe Thr Ile Lys Ser Asp Val 180 185 190 Trp Ser Phe Gly Ile Leu Leu Thr Glu Leu Thr Thr Lys Gly Arg Val 195 200 205 Pro Tyr Pro Gly Met Val Asn Arg Glu Val Leu Asp Gln Val Glu Arg 210 215 220 Gly Tyr Arg Met Pro Cys Pro Pro Glu Cys Pro Glu Ser Leu His Asp 225 230 235 240 Leu Met Cys Gln Cys Trp Arg Lys Glu Pro Glu Glu Arg Pro Thr Phe 245 250 255 Glu Tyr Leu Gln Ala Phe Leu Glu Asp Tyr Phe Thr Ser Thr Glu Pro 260 265 270 Gln 33 274 PRT Homo sapiens 33 Leu Pro His Trp Asp Asp Trp Glu Arg Pro Arg Glu Glu Phe Thr Leu 1 5 10 15 Cys Arg Lys Leu Gly Ser Gly Tyr Phe Gly Glu Val Phe Glu Gly Leu 20 25 30 Trp Lys Asp Arg Val Gln Val Ala Ile Lys Val Ile Ser Arg Asp Asn 35 40 45 Leu Leu His Gln Gln Met Leu Gln Ser Glu Ile Gln Ala Met Lys Lys 50 55 60 Leu Arg His Lys His Ile Leu Ala Leu Tyr Ala Val Val Ser Val Gly 65 70 75 80 Asp Pro Val Tyr Ile Ile Thr Glu Leu Met Ala Lys Gly Ser Leu Leu 85 90 95 Glu Leu Leu Arg Asp Ser Asp Glu Lys Val Leu Pro Val Ser Glu Leu 100 105 110 Leu Asp Ile Ala Trp Gln Val Ala Glu Gly Met Cys Tyr Leu Glu Ser 115 120 125 Gln Asn Tyr Ile His Arg Asp Leu Ala Ala Arg Asn Ile Leu Val Gly 130 135 140 Glu Asn Thr Leu Cys Lys Val Gly Asp Phe Gly Leu Ala Arg Leu Ile 145 150 155 160 Lys Glu Asp Val Tyr Leu Ser His Asp His Asn Ile Pro Tyr Lys Trp 165 170 175 Thr Ala Pro Glu Ala Leu Ser Arg Gly His Tyr Ser Thr Lys Ser Asp 180 185 190 Val Trp Ser Phe Gly Ile Leu Leu His Glu Met Phe Ser Arg Gly Gln 195 200 205 Val Pro Tyr Pro Gly Met Ser Asn His Glu Ala Phe Leu Arg Val Asp 210 215 220 Ala Gly Tyr Arg Met Pro Cys Pro Leu Glu Cys Pro Pro Ser Val His 225 230 235 240 Lys Leu Met Leu Thr Cys Trp Cys Arg Asp Pro Glu Gln Arg Pro Cys 245 250 255 Phe Lys Ala Leu Arg Glu Arg Leu Ser Ser Phe Thr Ser Tyr Glu Asn 260 265 270 Pro Thr 34 271 PRT Homo sapiens 34 Gly Leu Gly Tyr Gly Ser Trp Glu Ile Asp Pro Lys Asp Leu Thr Phe 1 5 10 15 Leu Lys Glu Leu Gly Thr Gly Gln Phe Gly Val Val Lys Tyr Gly Lys 20 25 30 Trp Arg Gly Gln Tyr Asp Val Ala Ile Lys Met Ile Lys Glu Gly Ser 35 40 45 Met Ser Glu Asp Glu Phe Ile Glu Glu Ala Lys Val Met Met Asn Leu 50 55 60 Ser His Glu Lys Leu Val Gln Leu Tyr Gly Val Cys Thr Lys Gln Arg 65 70 75 80 Pro Ile Phe Ile Ile Thr Glu Tyr Met Ala Asn Gly Cys Leu Leu Asn 85 90 95 Tyr Leu Arg Glu Met Arg His Arg Phe Gln Thr Gln Gln Leu Leu Glu 100 105 110 Met Cys Lys Asp Val Cys Glu Ala Met Glu Tyr Leu Glu Ser Lys Gln 115 120 125 Phe Leu His Arg Asp Leu Ala Ala Arg Asn Cys Leu Val Asn Asp Gln 130 135 140 Gly Val Val Lys Val Ser Asp Phe Gly Leu Ser Arg Tyr Val Leu Asp 145 150 155 160 Asp Glu Tyr Thr Ser Ser Val Gly Ser Lys Phe Pro Val Arg Trp Ser 165 170 175 Pro Pro Glu Val Leu Met Tyr Ser Lys Phe Ser Ser Lys Ser Asp Ile 180 185 190 Trp Ala Phe Gly Val Leu Met Trp Glu Ile Tyr Ser Leu Gly Lys Met 195 200 205 Pro Tyr Glu Arg Phe Thr Asn Ser Glu Thr Ala Glu His Ile Ala Gln 210 215 220 Gly Leu Arg Leu Tyr Arg Pro His Leu Ala Ser Glu Lys Val Tyr Thr 225 230 235 240 Ile Met Tyr Ser Cys Trp His Glu Lys Ala Asp Glu Arg Pro Thr Phe 245 250 255 Lys Ile Leu Leu Ser Asn Ile Leu Asp Val Met Asp Glu Glu Ser 260 265 270 35 269 PRT Homo sapiens 35 Glu Phe Tyr Arg Ser Gly Trp Ala Leu Asn Met Lys Glu Leu Lys Leu 1 5 10 15 Leu Gln Thr Ile Gly Lys Gly Glu Phe Gly Asp Val Met Leu Gly Asp 20 25 30 Tyr Arg Gly Asn Lys Val Ala Val Lys Cys Ile Lys Asn Asp Ala Thr 35 40 45 Ala Gln Ala Phe Leu Ala Glu Ala Ser Val Met Thr Gln Leu Arg His 50 55 60 Ser Asn Leu Val Gln Leu Leu Gly Val Ile Val Glu Glu Lys Gly Gly 65 70 75 80 Leu Tyr Ile Val Thr Glu Tyr Met Ala Lys Gly Ser Leu Val Asp Tyr 85 90 95 Leu Arg Ser Arg Gly Arg Ser Val Leu Gly Gly Asp Cys Leu Leu Lys 100 105 110 Phe Ser Leu Asp Val Cys Glu Ala Met Glu Tyr Leu Glu Gly Asn Asn 115 120 125 Phe Val His Arg Asp Leu Ala Ala Arg Asn Val Leu Val Ser Glu Asp 130 135 140 Asn Val Ala Lys Val Ser Asp Phe Gly Leu Thr Lys Glu Ala Ser Ser 145 150 155 160 Thr Gln Asp Thr Gly Lys Leu Pro Val Lys Trp Thr Ala Pro Glu Ala 165 170 175 Leu Arg Glu Lys Lys Phe Ser Thr Lys Ser Asp Val Trp Ser Phe Gly 180 185 190 Ile Leu Leu Trp Glu Ile Tyr Ser Phe Gly Arg Val Pro Tyr Pro Arg 195 200 205 Ile Pro Leu Lys Asp Val Val Pro Arg Val Glu Lys Gly Tyr Lys Met 210 215 220 Asp Ala Pro Asp Gly Cys Pro Pro Ala Val Tyr Glu Val Met Lys Asn 225 230 235 240 Cys Trp His Leu Asp Ala Ala Met Arg Pro Ser Phe Leu Gln Leu Arg 245 250 255 Glu Gln Leu Glu His Ile Lys Thr His Glu Leu His Leu 260 265 36 275 PRT Homo sapiens 36 Ser Pro Asn Tyr Asp Lys Trp Glu Met Glu Arg Thr Asp Ile Thr Met 1 5 10 15 Lys His Lys Leu Gly Gly Gly Gln Tyr Gly Glu Val Tyr Glu Gly Val 20 25 30 Trp Lys Lys Tyr Ser Leu Thr Val Ala Val Lys Thr Leu Lys Glu Asp 35 40 45 Thr Met Glu Val Glu Glu Phe Leu Lys Glu Ala Ala Val Met Lys Glu 50 55 60 Ile Lys His Pro Asn Leu Val Gln Leu Leu Gly Val Cys Thr Arg Glu 65 70 75 80 Pro Pro Phe Tyr Ile Ile Thr Glu Phe Met Thr Tyr Gly Asn Leu Leu 85 90 95 Asp Tyr Leu Arg Glu Cys Asn Arg Gln Glu Val Asn Ala Val Val Leu 100 105 110 Leu Tyr Met Ala Thr Gln Ile Ser Ser Ala Met Glu Tyr Leu Glu Lys 115 120 125 Lys Asn Phe Ile His Arg Asp Leu Ala Ala Arg Asn Cys Leu Val Gly 130 135 140 Glu Asn His Leu Val Lys Val Ala Asp Phe Gly Leu Ser Arg Leu Met 145 150 155 160 Thr Gly Asp Thr Tyr Thr Ala His Ala Gly Ala Lys Phe Pro Ile Lys 165 170 175 Trp Thr Ala Pro Glu Ser Leu Ala Tyr Asn Lys Phe Ser Ile Lys Ser 180 185 190 Asp Val Trp Ala Phe Gly Val Leu Leu Trp Glu Ile Ala Thr Tyr Gly 195 200 205 Met Ser Pro Tyr Pro Gly Ile Asp Leu Ser Gln Val Tyr Glu Leu Leu 210 215 220 Glu Lys Asp Tyr Arg Met Glu Arg Pro Glu Gly Cys Pro Glu Lys Val 225 230 235 240 Tyr Glu Leu Met Arg Ala Cys Trp Gln Trp Asn Pro Ser Asp Arg Pro 245 250 255 Ser Phe Ala Glu Ile His Gln Ala Phe Glu Thr Met Phe Gln Glu Ser 260 265 270 Ser Ile Ser 275 37 279 PRT Homo sapiens 37 Leu Lys Asp Lys Lys Leu Phe Leu Lys Arg Asp Asn Leu Leu Ile Ala 1 5 10 15 Asp Ile Glu Leu Gly Cys Gly Asn Phe Gly Ser Val Arg Gln Gly Val 20 25 30 Tyr Arg Met Arg Lys Lys Gln Ile Asp Val Ala Ile Lys Val Leu Lys 35 40 45 Gln Gly Thr Glu Lys Ala Asp Thr Glu Glu Met Met Arg Glu Ala Gln 50 55 60 Ile Met His Gln Leu Asp Asn Pro Tyr Ile Val Arg Leu Ile Gly Val 65 70 75 80 Cys Gln Ala Glu Ala Leu Met Leu Val Met Glu Met Ala Gly Gly Gly 85 90 95 Pro Leu His Lys Phe Leu Val Gly Lys Arg Glu Glu Ile Pro Val Ser 100 105 110 Asn Val Ala Glu Leu Leu His Gln Val Ser Met Gly Met Lys Tyr Leu 115 120 125 Glu Glu Lys Asn Phe Val His Arg Asp Leu Ala Ala Arg Asn Val Leu 130 135 140 Leu Val Asn Arg His Tyr Ala Lys Ile Ser Asp Phe Gly Leu Ser Lys 145 150 155 160 Ala Leu Gly Ala Asp Asp Ser Tyr Tyr Thr Ala Arg Ser Ala Gly Lys 165 170 175 Trp Pro Leu Lys Trp Tyr Ala Pro Glu Cys Ile Asn Phe Arg Lys Phe 180 185 190 Ser Ser Arg Ser Asp Val Trp Ser Tyr Gly Cys Thr Met Trp Glu Ala 195 200 205 Leu Ser Tyr Gly Gln Lys Pro Tyr Lys Lys Met Lys Gly Pro Glu Val 210 215 220 Met Ala Phe Ile Glu Gln Gly Lys Arg Met Glu Cys Pro Pro Glu Cys 225 230 235 240 Pro Pro Glu Leu Tyr Ala Leu Met Ser Asp Cys Trp Ile Tyr Lys Trp 245 250 255 Glu Asp Arg Pro Asp Phe Leu Thr Val Glu Gln Arg Met Arg Ala Cys 260 265 270 Tyr Tyr Ser Leu Ala Ser Lys 275 38 275 PRT Homo sapiens 38 Ala Val Pro Lys Asp Lys Trp Val Leu Asn His Glu Asp Leu Val Leu 1 5 10 15 Gly Glu Gln Ile Gly Arg Gly Asn Phe Gly Glu Val Phe Ser Gly Arg 20 25 30 Leu Arg Ala Asp Asn Thr Leu Val Ala Val Lys Ser Cys Arg Glu Thr 35 40 45 Leu Pro Pro Asp Leu Lys Ala Lys Phe Leu Gln Glu Ala Arg Ile Leu 50 55 60 Lys Gln Tyr Ser His Pro Asn Ile Val Arg Leu Ile Gly Val Cys Thr 65 70 75 80 Gln Lys Gln Pro Ile Tyr Ile Val Met Glu Leu Val Gln Gly Gly Asp 85 90 95 Phe Leu Thr Phe Leu Arg Thr Glu Gly Ala Arg Leu Arg Val Lys Thr 100 105 110 Leu Leu Gln Met Val Gly Asp Ala Ala Ala Gly Met Glu Tyr Leu Glu 115 120 125 Ser Lys Cys Cys Ile His Arg Asp Leu Ala Ala Arg Asn Cys Leu Val 130 135 140 Thr Glu Lys Asn Val Leu Lys Ile Ser Asp Phe Gly Met Ser Arg Glu 145 150 155 160 Glu Ala Asp Gly Val Tyr Ala Ala Ser Gly Gly Ser Arg Gln Val Pro 165 170 175 Val Lys Trp Thr Ala Pro Glu Ala Leu Asn Tyr Gly Arg Tyr Ser Ser 180 185 190 Glu Ser Asp Val Trp Ser Phe Gly Ile Leu Leu Trp Glu Thr Phe Ser 195 200 205 Leu Gly Ala Ser Pro Tyr Pro Asn Leu Ser Asn Gln Gln Thr Arg Glu 210 215 220 Phe Val Glu Lys Gly Gly Arg Leu Pro Cys Pro Glu Leu Cys Pro Asp 225 230 235 240 Ala Val Phe Arg Leu Met Glu Gln Cys Trp Ala Tyr Glu Pro Gly Gln 245 250 255 Arg Pro Ser Phe Ser Thr Ile Tyr Gln Glu Leu Gln Ser Ile Arg Lys 260 265 270 Arg His Arg 275 39 278 PRT Homo sapiens 39 Met Pro Ser Thr Arg Asp Tyr Glu Ile Gln Arg Glu Arg Ile Glu Leu 1 5 10 15 Gly Arg Cys Ile Gly Glu Gly Gln Phe Gly Asp Val His Gln Gly Ile 20 25 30 Tyr Met Ser Pro Glu Asn Pro Ala Leu Ala Val Ala Ile Lys Thr Cys 35 40 45 Lys Asn Cys Thr Ser Asp Ser Val Arg Glu Lys Phe Leu Gln Glu Ala 50 55 60 Leu Thr Met Arg Gln Phe Asp His Pro His Ile Val Lys Leu Ile Gly 65 70 75 80 Val Ile Thr Glu Asn Pro Val Trp Ile Ile Met Glu Leu Cys Thr Leu 85 90 95 Gly Glu Leu Arg Ser Phe Leu Gln Val Arg Lys Tyr Ser Leu Asp Leu 100 105 110 Ala Ser Leu Ile Leu Tyr Ala Tyr Gln Leu Ser Thr Ala Leu Ala Tyr 115 120 125 Leu Glu Ser Lys Arg Phe Val His Arg Asp Ile Ala Ala Arg Asn Val 130 135 140 Leu Val Ser Ser Asn Asp Cys Val Lys Leu Gly Asp Phe Gly Leu Ser 145 150 155 160 Arg Tyr Met Glu Asp Ser Thr Tyr Tyr Lys Ala Ser Lys Gly Lys Leu 165 170 175 Pro Ile Lys Trp Met Ala Pro Glu Ser Ile Asn Phe Arg Arg Phe Thr 180 185 190 Ser Ala Ser Asp Val Trp Met Phe Gly Val Cys Met Trp Glu Ile Leu 195 200 205 Met His Gly Val Lys Pro Phe Gln Gly Val Lys Asn Asn Asp Val Ile 210 215 220 Gly Arg Ile Glu Asn Gly Glu Arg Leu Pro Met Pro Pro Asn Cys Pro 225 230 235 240 Pro Thr Leu Tyr Ser Leu Met Thr Lys Cys Trp Ala Tyr Asp Pro Ser 245 250 255 Arg Arg Pro Arg Phe Thr Glu Leu Lys Ala Gln Leu Ser Thr Ile Leu 260 265 270 Glu Glu Glu Lys Ala Gln 275 40 292 PRT Homo sapiens 40 Pro Thr Glu Val Asp Pro Thr His Phe Glu Lys Arg Phe Leu Lys Arg 1 5 10 15 Ile Arg Asp Leu Gly Glu Gly His Phe Gly Lys Val Glu Leu Cys Arg 20 25 30 Tyr Asp Pro Glu Asp Asn Thr Gly Glu Gln Val Ala Val Lys Ser Leu 35 40 45 Lys Pro Glu Ser Gly Gly Asn His Ile Ala Asp Leu Lys Lys Glu Ile 50 55 60 Glu Ile Leu Arg Asn Leu Tyr His Glu Asn Ile Val Lys Tyr Lys Gly 65 70 75 80 Ile Cys Thr Glu Asp Gly Gly Asn Gly Ile Lys Leu Ile Met Glu Phe 85 90 95 Leu Pro Ser Gly Ser Leu Lys Glu Tyr Leu Pro Lys Asn Lys Asn Lys 100 105 110 Ile Asn Leu Lys Gln Gln Leu Lys Tyr Ala Val Gln Ile Cys Lys Gly 115 120 125 Met Asp Tyr Leu Gly Ser Arg Gln Tyr Val His Arg Asp Leu Ala Ala 130 135 140 Arg Asn Val Leu Val Glu Ser Glu His Gln Val Lys Ile Gly Asp Phe 145 150 155 160 Gly Leu Thr Lys Ala Ile Glu Thr Asp Lys Glu Tyr Tyr Thr Val Lys 165 170 175 Asp Asp Arg Asp Ser Pro Val Phe Trp Tyr Ala Pro Glu Cys Leu Met 180 185 190 Gln Ser Lys Phe Tyr Ile Ala Ser Asp Val Trp Ser Phe Gly Val Thr 195 200 205 Leu His Glu Leu Leu Thr Tyr Cys Asp Ser Asp Ser Ser Pro Met Ala 210 215 220 Leu Phe Leu Lys Met Ile Gly Pro Thr His Gly Gln Met Thr Val Thr 225 230 235 240 Arg Leu Val Asn Thr Leu Lys Glu Gly Lys Arg Leu Pro Cys Pro Pro 245 250 255 Asn Cys Pro Asp Glu Val Tyr Gln Leu Met Arg Lys Cys Trp Glu Phe 260 265 270 Gln Pro Ser Asn Arg Thr Ser Phe Gln Asn Leu Ile Glu Gly Phe Glu 275 280 285 Ala Leu Leu Lys 290 41 283 PRT Homo sapiens 41 Pro Leu Gln Ser Leu Thr Cys Leu Ile Gly Glu Lys Asp Leu Arg Leu 1 5 10 15 Leu Glu Lys Leu Gly Asp Gly Ser Phe Gly Val Val Arg Arg Gly Glu 20 25 30 Trp Asp Ala Pro Ser Gly Lys Thr Val Ser Val Ala Val Lys Cys Leu 35 40 45 Lys Pro Asp Val Leu Ser Gln Pro Glu Ala Met Asp Asp Phe Ile Arg 50 55 60 Glu Val Asn Ala Met His Ser Leu Asp His Arg Asn Leu Ile Arg Leu 65 70 75 80 Tyr Gly Val Val Leu Thr Pro Pro Met Lys Met Val Thr Glu Leu Ala 85 90 95 Pro Leu Gly Ser Leu Leu Asp Arg Leu Arg Lys His Gln Gly His Phe 100 105 110 Leu Leu Gly Thr Leu Ser Arg Tyr Ala Val Gln Val Ala Glu Gly Met 115 120 125 Gly Tyr Leu Glu Ser Lys Arg Phe Ile His Arg Asp Leu Ala Ala Arg 130 135 140 Asn Leu Leu Leu Ala Thr Arg Asp Leu Val Lys Ile Gly Asp Phe Gly 145 150 155 160 Leu Met Arg Ala Leu Pro Gln Asn Asp Asp His Tyr Val Met Gln Glu 165 170 175 His Arg Lys Val Pro Phe Ala Trp Cys Ala Pro Glu Ser Leu Lys Thr 180 185 190 Arg Thr Phe Ser His Ala Ser Asp Thr Trp Met Phe Gly Val Thr Leu 195 200 205 Trp Glu Met Phe Thr Tyr Gly Gln Glu Pro Trp Ile Gly Leu Asn Gly 210 215 220 Ser Gln Ile Leu His Lys Ile Asp Lys Glu Gly Glu Arg Leu Pro Arg 225 230 235 240 Pro Glu Asp Cys Pro Gln Asp Ile Tyr Asn Val Met Val Gln Cys Trp 245 250 255 Ala His Lys Pro Glu Asp Arg Pro Thr Phe Val Ala Leu Arg Asp Phe 260 265 270 Leu Leu Glu Ala Gln Pro Thr Asp Met Arg Ala 275 280 

What is claimed is:
 1. A crystalline form of a polypeptide corresponding to the catalytic domain of a non-insulin receptor tyrosine kinase.
 2. The crystalline polypeptide of claim 1 in which the non-insulin receptor tyrosine kinase is a receptor tyrosine kinase.
 3. The crystalline polypeptide of claim 1 in which the non-insulin receptor tyrosine kinase is a cytoplasmic tyrosine kinase.
 4. The crystalline polypeptide of claim 2 in which the non-insulin receptor tyrosine kinase is FGF-R, PDGF-R, KDR, CCK4, MET, TRKA, AXL, TIE, EPH, RYK, DDR, ROS, RET, LTK, ROR1, or MUSK.
 5. The crystalline polypeptide of claim 3 in which the cytoplasmic tyrosine kinase is SRC, BRK, BTK; CSK, ABL, ZAP70, FES, FAK, JAK, or ACK.
 6. A derivative crystal comprising the crystalline form of the polypeptide of claim 1, 2, 3, 4 or 5 in a covalent association with a heavy metal atom.
 7. A co-crystal comprising the crystalline form of the polypeptide of claim 1, 2, 3, 4 or 5 in association with a compound such as a cofactor, substrate, substrate analog, inhibitor, or allosteric effector.
 8. The co-crystal of claim 7 in which the compound is a non-hydrolyzable analog of ATP.
 9. A crystal of an FGF receptor tyrosine kinase domain protein, wherein the crystal is characterized by having monoclinic unit cells and space group symmetry C2.
 10. The crystal of claim 9, wherein the FGF receptor tyrosine kinase domain protein is FLGK.
 11. The FLGK crystal of claim 10, wherein the monoclinic unit cells have dimensions of about a=208.3±0.2 Å, b=57.8±0.2 Å, c=65.5±0.2 Å and β=107.2°±0.2°.
 12. The FLGK crystal of claim 10, wherein the monoclinic unit cells have dimensions of about a=211.6±0.2 Å, b=51.3±0.2 Å, c=66.1±0.2 Å and β=107.7°±0.2°.
 13. The FLGK crystal of claim 10, wherein the crystal is a native crystal.
 14. The native FLGK crystal of claim 13, wherein the FLGK has a three-dimensional structure characterized by the atomic structure coordinates of Table
 3. 15. The FLGK crystal of claim 10, wherein the crystal is a heavy atom derivative crystal.
 16. The FLGK crystal of claim 10, wherein the crystal is a co-crystal.
 17. The co-crystal of claim 16, wherein the FLGK protein has a three-dimensional structure characterized by the atomic structure coordinates of Table
 4. 18. A polypeptide corresponding to the catalytic domain of a non-insulin receptor tyrosine kinase, containing at least about 20 amino acid residues upstream of the first glycine in the conserved glycine-rich region of the catalytic domain, and at least about 17 amino acid residues downstream of the conserved arginine located at the C-terminal boundary of the catalytic domain.
 19. The polypeptide of claim 18 in which the non-insulin receptor tyrosine kinase is a receptor tyrosine kinase.
 20. The polypeptide of claim 18 in which the non-insulin receptor tyrosine kinase is a cytoplasmic tyrosine kinase.
 21. The polypeptide of claim 18 in which the non-insulin receptor tyrosine kinase is FGF-R, PDGF-R, KDR, CCK4, MET, TRKA, AXL, TIE, EPH, RYK, DDR, ROS, RET, LTK, ROR1, or MUSK.
 22. The polypeptide of claim 20 in which the cytoplasmic kinase is SRC, BRK, BTK, CSK, ABL, ZAP70, FES, FAK, JAK, or ACK.
 23. The polypeptide of claim 21 or 22 having the amino acid sequence shown in FIGS. 6A or 6B.
 24. A method of-using the polypeptide of claim 18, 19, 20, 21 or 22 to form a crystal, comprising: (a) mixing a volume of polypeptide solution with a reservoir solution; and (b) incubating the mixture obtained in step (a) over the reservoir solution in a closed container, under conditions suitable for crystallization.
 25. A method of obtaining FGF receptor tyrosine kinase domain polypeptide in crystalline form, the method comprising the steps of: (a) mixing a volume of polypeptide solution with an equal volume of reservoir solution, wherein the polypeptide solution comprises 1 mg/mL to 60 mg/mL FGF-type tyrosine kinase domain protein, 10 mM to 200 mM buffering agent, 0 mM to 20 mM dithiothreitol and has a pH of about 5.5 to about 7.5, and wherein the reservoir solution comprises 10% to 30% (w/v) polyethylene glycol, 0.1 M to 0.5 M ammonium sulfate, 0% to 20% (w/v) ethylene glycol or glycerol, 10 mM to 200 mM buffering agent and has a pH of about 5.5 to about 7.5; and (b) incubating the mixture obtained in step (a) over said reservoir solution in a closed container at a temperature between 0° and 25° until crystals form.
 26. The method of claim 25, wherein the polypeptide solution comprises about 10 mg/mL FGF receptor tyrosine kinase domain, about 10 mM sodium chloride, about 2 mM dithiothreitol, about 10 mM Tris-HCl and has a pH of about 8; the reservoir buffer comprises about 16% (w/v) polyethylene glycol (MW 10000), about 0.3 M ammonium sulfate, about 5%. ethylene glycol or glycerol, about 100 mM bis-Tris and has a pH of about 6.5; and the temperature is about 4° C.
 27. The method of claim 25, wherein the polypeptide solution includes a compound such as a cofactor, substrate, substrate analog, inhibitor or allosteric effector.
 28. The method of claim 25, wherein the compound is a non-hydrolyzable analog of ATP.
 29. A cDNA encoding an FGF receptor tyrosine kinase domain protein, wherein a coding strand of the cDNA has the nucleotide sequence of SEQ ID NO:5. 